Entry ID
stringlengths
4
4
Experimental Method
stringclasses
2 values
Matthews Coefficient
float64
0.41
7.24
Percent Solvent Content
float64
0.47
83
Crystallization Method
stringclasses
15 values
pH
float64
3
11
Crystal Growth Procedure
stringlengths
3
1.23k
Temp (K)
float64
273
316
Deposition Date
stringdate
2013-04-23 00:00:00
2024-08-20 00:00:00
Release Date
stringdate
2015-01-07 00:00:00
2024-09-11 00:00:00
Number of Non-Hydrogen Atoms per Deposited Model
float64
395
50.9k
Total Number of Polymer Instances (Chains)
float64
1
42
Total Number of Polymer Residues per Deposited Model
float64
39
6.96k
Number of Water Molecules per Deposited Model
float64
1
3.43k
Disulfide Bond Count per Deposited Model
float64
1
73
Molecular Weight per Deposited Model
float64
4.98
778
Number of Distinct Protein Entities
float64
1
15
Refinement Resolution (Å)
stringlengths
1
13
Structure Determination Methodology
stringclasses
1 value
Average B Factor
float64
6.66
145
R Free
float64
0.12
0.38
R Work
float64
0.1
0.32
Structure Title
stringlengths
7
292
Sequence
stringlengths
3
2.13k
Entity Polymer Type
stringclasses
3 values
Polymer Entity Sequence Length
float64
3
2.13k
Entity Macromolecule Type
stringclasses
4 values
Total Number of polymer Entity Instances (Chains) per Entity
float64
1
12
Molecular Weight (Entity)
float64
0.23
241
Macromolecule Name
stringlengths
3
299
EC Number
stringclasses
444 values
EC Provenance Source
stringclasses
1 value
Source Organism
stringclasses
76 values
Taxonomy ID
float64
274
3.05M
Total Number of Polymer Residues per Assembly
float64
23
6.96k
Total Number of Polymer Instances (Chains) per Assembly
float64
1
34
Oligomeric Count
float64
1
34
Assembly ID
float64
1
1
Oligomeric State
stringclasses
20 values
Stoichiometry
stringclasses
38 values
Ligand ID
stringlengths
1
5
Ligand Formula
stringlengths
1
22
Ligand MW
float64
16
1.77k
Ligand Name
stringlengths
4
573
InChI
stringlengths
14
556
Ligand SMILES
stringlengths
1
207
Ligand of Interest
stringclasses
1 value
__index_level_0__
int64
1
11.8k
7CMB
X-RAY DIFFRACTION
2.78
55.78
VAPOR DIFFUSION
8.5
0.2M Ammonium sulfate, 0.1M Tris pH 8.5, 25% PEG3350
291
2020-07-26
2021-07-28
2,333
1
293
4
null
33.47
1
2.592
experimental
75.003
0.2509
0.2059
Crystal Structure of PAK4 in complex with inhibitor 41
SSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
Protein
293
polypeptide(L)
1
33.098
Serine/threonine-protein kinase PAK 4
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
293
1
1
1
Monomer
A1
G5X
C21 H21 N5 O2
375.424
1-(2-azanylpyrimidin-4-yl)-6-[2-(1-oxidanylcyclohexyl)ethynyl]indole-3-carboxamide
InChI=1S/C21H21N5O2/c22-19(27)16-13-26(18-7-11-24-20(23)25-18)17-12-14(4-5-15(16)17)6-10-21(28)8-2-1-3-9-21/h4-5,7,11-13,28H,1-3,8-9H2,(H2,22,27)(H2,23,24,25)
c1cc2c(cc1C#CC3(CCCCC3)O)n(cc2C(=O)N)c4ccnc(n4)N
Y
2,865
5CTP
X-RAY DIFFRACTION
2.25
45.44
VAPOR DIFFUSION, HANGING DROP
6.5
107mM Mes pH 6.5, 29% glycerol ethoxylate, 1 M ammonium acetate
298
2015-07-24
2016-11-30
5,831
2
704
212
null
83.9
1
2.033
experimental
56.12
0.1989
0.1848
Crystal structure of CK2alpha with N-(3-(3-chloro-4-(phenyl)benzylamino)propyl)acetamide bound
GSMDIEFDDDADDDGSGSGSGSGSSGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVK
Protein
352
polypeptide(L)
2
41.468
Casein kinase II subunit alpha
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
352
1
1
1
Monomer
A1
ACT
C2 H3 O2
59.044
ACETATE ION
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
CC(=O)[O-]
null
3,721
6L5N
X-RAY DIFFRACTION
2.6
52.74
VAPOR DIFFUSION, SITTING DROP
7.5
7% MPD and 0.1M Bicine, pH8.5
293
2019-10-24
2020-06-17
6,518
4
784
156
null
95.63
1
2.242
experimental
37.7253
0.233
0.1753
Crystal structure of human DEAD-box RNA helicase DDX21 at post-unwound state
SFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHWTQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITLKGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICFYQHKEEYQLVQVEQKAGIKFKRI
Protein
377
polypeptide(L)
2
42.471
Nucleolar RNA helicase 2
3.6.4.13
PDB Primary Data
Homo sapiens
9,606
392
2
2
1
Monomer
A1
ANP
C10 H17 N6 O12 P3
506.196
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
InChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
Y
6,377
6VNY
X-RAY DIFFRACTION
1.85
33.64
EVAPORATION
8
0.1 M bis-tris pH 5.5, 0.25 M NaCl, 10 mM TCEP, 27-33% PEG-3350
298
2020-01-29
2020-04-08
2,470
1
318
131
null
36.94
1
2.3
experimental
40.75
0.2292
0.1736
Crystal structure of TYK2 kinase with compound 10
MAHHHHHHHHHHGALEVLFQGPGDPTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADAGPQHRSGWKQEIDILRTLYHEHIIKYKGCCEDAGAASLQLVMEYVPLGSLRDYLPRHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLELIGIAQGQMTVLRLTELLERGERLPRPDKCPAEVYHLMKNCWETEASFRPTFENLIPILKTVHEKYQGQAPS
Protein
318
polypeptide(L)
1
36.551
Non-receptor tyrosine-protein kinase TYK2
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
318
1
1
1
Monomer
A1
R4S
C18 H22 F N7 O2
387.411
N-[(1S,5R)-3-(5-fluoro-2-{[1-(2-hydroxyethyl)-1H-pyrazol-4-yl]amino}pyrimidin-4-yl)-3-azabicyclo[3.1.0]hexan-1-yl]cyclopropanecarboxamide
InChI=1S/C18H22FN7O2/c19-14-7-20-17(22-13-6-21-26(9-13)3-4-27)23-15(14)25-8-12-5-18(12,10-25)24-16(28)11-1-2-11/h6-7,9,11-12,27H,1-5,8,10H2,(H,24,28)(H,20,22,23)/t12-,18-/m1/s1
c1c(cn(n1)CCO)Nc2ncc(c(n2)N3CC4CC4(C3)NC(=O)C5CC5)F
Y
2,291
6WBW
X-RAY DIFFRACTION
2.43
49.43
VAPOR DIFFUSION, HANGING DROP
null
25% PEG 3350, 0.2 M ammonium sulfate, 0.1 M Hepes pH 7.5
293
2020-03-27
2020-05-06
10,250
3
1,128
1,121
null
131.75
1
1.46
experimental
26.28
0.197
0.172
Structure of Human HDAC2 in complex with an ethyl ketone inhibitor
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPH
Protein
376
polypeptide(L)
3
43.062
Histone deacetylase 2
3.5.1.98
PDB Primary Data
Homo sapiens
9,606
376
1
1
1
Monomer
A1
TV1
C27 H37 N5 O4
495.614
N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide
InChI=1S/C27H37N5O4/c1-4-27(34,35)13-9-5-6-12-22(30-25(33)19-16-32(2)17-19)24-28-15-23(29-24)20-14-18-10-7-8-11-21(18)31-26(20)36-3/h7-8,10-11,14-15,19,22,34-35H,4-6,9,12-13,16-17H2,1-3H3,(H,28,29)(H,30,33)/t22-/m0/s1
CCC(CCCCCC(c1[nH]c(cn1)c2cc3ccccc3nc2OC)NC(=O)C4CN(C4)C)(O)O
Y
10,190
4Z6F
X-RAY DIFFRACTION
2.25
45.34
VAPOR DIFFUSION, SITTING DROP
7.5
14% to 23% PEG3400, and 350 mM sodium acetate in 50 mM imidazole (pH 7.5)
298
2015-04-04
2016-04-13
3,350
4
366
79
null
48.31
1
2.444
experimental
null
0.2483
0.1949
Structure of human DNA polymerase beta 279NA mutant complexed with G in the template base paired with incoming non-hydrolyzable TTP and MANGANESE
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFAKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
Protein
335
polypeptide(L)
1
38.199
DNA polymerase beta
2.7.7.7
PDB Primary Data
Homo sapiens
9,606
366
4
4
1
Monomer
A1
MN
Mn
54.938
MANGANESE (II) ION
InChI=1S/Mn/q+2
[Mn+2]
null
83
4QMV
X-RAY DIFFRACTION
2.55
51.71
VAPOR DIFFUSION, HANGING DROP
7.5
12.5 mg/mL MST3, 1 mM PF-03814735, 25 mM TRIS, PH 8.0, 50 MM HEPES pH 7.5, 125 mM SODIUM CHLORIDE, 100 mM MAGNESIUM CHLORIDE, 15% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 291K
291
2014-06-16
2015-07-01
2,448
1
310
91
null
35.62
1
2.4
experimental
null
0.2264
0.1674
MST3 IN COMPLEX WITH PF-03814735, N-{2-[(1S,4R)-6-{[4-(CYCLOBUTYLAMINO)-5-(TRIFLUOROMETHYL)PYRIMIDIN-2-YL]AMINO}-1,2,3,4-TETRAHYDRO-1,4-EPIMINONAPHTHALEN-9-YL]-2-OXOETHYL}ACETAMIDE
GPLGSEFMAHSPVQSGLPGMQNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDS
Protein
310
polypeptide(L)
1
35.024
SERINE/THREONINE-PROTEIN KINASE 24
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
310
1
1
1
Monomer
A1
34W
C23 H25 F3 N6 O2
474.479
N-{2-[(1S,4R)-6-{[4-(cyclobutylamino)-5-(trifluoromethyl)pyrimidin-2-yl]amino}-1,2,3,4-tetrahydro-1,4-epiminonaphthalen-9-yl]-2-oxoethyl}acetamide
InChI=1S/C23H25F3N6O2/c1-12(33)27-11-20(34)32-18-7-8-19(32)16-9-14(5-6-15(16)18)30-22-28-10-17(23(24,25)26)21(31-22)29-13-3-2-4-13/h5-6,9-10,13,18-19H,2-4,7-8,11H2,1H3,(H,27,33)(H2,28,29,30,31)/t18-,19+/m0/s1
CC(=O)NCC(=O)N1C2CCC1c3c2ccc(c3)Nc4ncc(c(n4)NC5CCC5)C(F)(F)F
null
5,146
7V8F
X-RAY DIFFRACTION
1.98
36.94
EVAPORATION
8
2%(v/v) 1,4-dioxane, 0.1 M Tris-HCl (pH 8.0), 15%(w/v) PEG 3,350.
289
2021-08-22
2022-03-30
2,160
2
261
192
null
29.96
2
1.66
experimental
30.76
0.198
0.1753
Crystal structure of UBE2L3 bound to HOIP RING1 domain.
GPGSEFQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRD
Protein
103
polypeptide(L)
1
11.637
E3 ubiquitin-protein ligase RNF31
2.3.2.31
PDB Primary Data
Homo sapiens
9,606
261
2
2
1
Hetero 2-mer
A1, B1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
6,984
5R5E
X-RAY DIFFRACTION
2.02
39
VAPOR DIFFUSION, SITTING DROP
7.5
0.1M HEPES pH 7.5, 0.3M sodium/potassium phosphate, 15% PEG Smear High, 20% ethylene glycol
277
2020-02-28
2020-07-01
2,444
1
304
161
null
33.23
1
1.58
experimental
26.243
0.2245
0.1888
PanDDA analysis group deposition -- Crystal Structure of human NUDT22 in complex with N13848a
SMDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVRRLPETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
Protein
304
polypeptide(L)
1
32.707
Uridine diphosphate glucose pyrophosphatase NUDT22
3.6.1.45
PDB Primary Data
Homo sapiens
9,606
304
1
1
1
Monomer
A1
GV1
C10 H13 N3 S
207.295
~{N},~{N},5,6-tetramethylthieno[2,3-d]pyrimidin-4-amine
InChI=1S/C10H13N3S/c1-6-7(2)14-10-8(6)9(13(3)4)11-5-12-10/h5H,1-4H3
Cc1c(sc2c1c(ncn2)N(C)C)C
null
1,945
9FLT
X-RAY DIFFRACTION
3.16
61.01
VAPOR DIFFUSION, SITTING DROP
6.5
45% MPD 0.1M SPG 6.5
278
2024-06-05
2024-09-11
2,643
1
336
66
null
38.62
1
2.4
experimental
54.563
0.23881
0.18392
Crystal structure of human Haspin (GSG2) kinase bound to chemical probe MU1920
SMGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK
Protein
336
polypeptide(L)
1
38.24
Serine/threonine-protein kinase haspin
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
336
1
1
1
Monomer
A1
A1IDF
C17 H15 N5 S
321.4
~{N}-(1,4-dimethylpyrazol-3-yl)-3-pyridin-4-yl-thieno[3,2-b]pyridin-5-amine
InChI=1S/C17H15N5S/c1-11-9-22(2)21-17(11)20-15-4-3-14-16(19-15)13(10-23-14)12-5-7-18-8-6-12/h3-10H,1-2H3,(H,19,20,21)
Cc1cn(nc1Nc2ccc3c(n2)c(cs3)c4ccncc4)C
Y
1,649
5T53
X-RAY DIFFRACTION
3.89
68.37
VAPOR DIFFUSION, HANGING DROP
7.5
8% PEG 8000, 0.1M HEPES, pH 7.5 and 10 % ethylene glycol
298.15
2016-08-30
2016-11-09
1,436
1
227
14
null
27.12
1
2.699
experimental
null
0.2852
0.2496
MOLECULAR BASIS FOR COHESIN ACETYLATION BY ESTABLISHMENT OF SISTER CHROMATID COHESION N-ACETYLTRANSFERASE ESCO1
KTDEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGT
Protein
227
polypeptide(L)
1
26.248
N-acetyltransferase ESCO1
2.3.1
PDB Primary Data
Homo sapiens
9,606
227
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
4,176
6Q7K
X-RAY DIFFRACTION
2.28
45.95
VAPOR DIFFUSION, SITTING DROP
7.2
0.2M (NH4)2SO4 33% MPEG 2000 0.02M Mercaptoethanol 0.1M pH=7.2 HEPES/NaOH
293
2018-12-13
2019-03-27
3,103
1
368
284
null
42.73
1
1.84
experimental
34.718
0.26315
0.21091
ERK2 mini-fragment binding
MAHHHHHHMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
Protein
368
polypeptide(L)
1
42.552
Mitogen-activated protein kinase 1
2.7.11.24
PDB Primary Data
Homo sapiens
9,606
368
1
1
1
Monomer
A1
SO4
O4 S
96.063
SULFATE ION
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
[O-]S(=O)(=O)[O-]
null
10,656
8SLU
X-RAY DIFFRACTION
2.56
52.01
VAPOR DIFFUSION, SITTING DROP
5.65
30% PEG 3350, 200 mM Li2SO4, 100 mM bis-tris pH 5.65
293.15
2023-04-24
2023-06-21
2,547
1
282
98
null
32.8
1
1.84
experimental
41.64
0.2366
0.1948
Crystal structure of human STEP (PTPN5) at cryogenic temperature (100 K) and high pressure (205 MPa)
SMSRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSH
Protein
282
polypeptide(L)
1
32.518
Tyrosine-protein phosphatase non-receptor type 5
3.1.3.48
PDB Primary Data
Homo sapiens
9,606
282
1
1
1
Monomer
A1
SO4
O4 S
96.063
SULFATE ION
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
[O-]S(=O)(=O)[O-]
null
2,724
6GUU
X-RAY DIFFRACTION
3.8
67.61
VAPOR DIFFUSION, HANGING DROP
null
0.2 M ammonium nitrate 20 % PEG 3350 2 % benzamidine hydrochloride
277
2018-06-19
2019-10-09
3,394
2
482
null
null
57.43
1
2.95
experimental
117.22
0.263
0.2063
Structure of CHD5 PHD2 - tandem chromodomains
GPGEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELML
Protein
241
polypeptide(L)
2
28.586
Chromodomain-helicase-DNA-binding protein 5
3.6.4.12
PDB Primary Data
Homo sapiens
9,606
241
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
6,725
6WTN
X-RAY DIFFRACTION
2.09
41.16
VAPOR DIFFUSION, HANGING DROP
5
1.6-2.4 M sodium malonate, pH 5
291
2020-05-03
2021-05-05
2,416
1
309
93
null
36.9
1
1.83
experimental
41.6108
0.2084
0.1872
Human JAK2 JH1 domain in complex with Ruxolitinib
MAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAGGSGSENLYFQ
Protein
309
polypeptide(L)
1
36.412
Tyrosine-protein kinase JAK2
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
309
1
1
1
Monomer
A1
EDO
C2 H6 O2
62.068
1,2-ETHANEDIOL
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
C(CO)O
null
10,132
7RBH
X-RAY DIFFRACTION
2.24
45.15
VAPOR DIFFUSION, HANGING DROP
5.5
0.1 M Citrate pH 5.5, 18% PEG6000
298
2021-07-06
2022-03-09
3,646
4
372
288
null
49.89
1
1.75
experimental
32.189
0.2245
0.1793
Human DNA polymerase beta crosslinked ternary complex 2
GCTGATGCGC
DNA
10
polydeoxyribonucleotide
1
3.061
DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*C)-3')
null
null
synthetic construct
32,630
372
4
4
1
Monomer
A1
QPJ
C5 H14 O10 P2
296.106
2-deoxy-3,5-di-O-phosphono-D-erythro-pentitol
InChI=1S/C5H14O10P2/c6-2-1-5(15-17(11,12)13)4(7)3-14-16(8,9)10/h4-7H,1-3H2,(H2,8,9,10)(H2,11,12,13)/t4-,5+/m1/s1
C(CO)C(C(COP(=O)(O)O)O)OP(=O)(O)O
Y
414
7XMK
X-RAY DIFFRACTION
2.35
47.67
VAPOR DIFFUSION, HANGING DROP
null
0.25M ammonium iodide, 0.03M glycyl-glycyl-glycine, 23% polyethylene glycol (PEG) 3350
277
2022-04-26
2023-04-26
4,333
2
588
141
null
68.18
1
2.376
experimental
39.648
0.2585
0.2243
Crystal structure of human RIPK1 kinase domain in complex with compound SKLB923
MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
Protein
294
polypeptide(L)
2
33.469
Receptor-interacting serine/threonine-protein kinase 1
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
588
2
2
1
Homo 2-mer
A2
IOD
I
126.904
IODIDE ION
InChI=1S/HI/h1H/p-1
[I-]
null
11,238
8AWK
X-RAY DIFFRACTION
2.45
49.81
VAPOR DIFFUSION, SITTING DROP
7
0.2 M Na2SO4, 14% (v/v) PEG3350, 0.25 M HEPES pH 7.0
293
2022-08-30
2024-03-13
4,872
1
497
547
2
58.61
1
1.58
experimental
19.369
0.1849
0.1515
Structure of recombinant human beta-glucocerebrosidase in complex with D-carbaxylosyl chloride
ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
Protein
497
polypeptide(L)
1
55.659
Lysosomal acid glucosylceramidase
3.2.1.45
PDB Primary Data
Homo sapiens
9,606
497
1
1
1
Monomer
A1
SO4
O4 S
96.063
SULFATE ION
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
[O-]S(=O)(=O)[O-]
null
2,450
6C90
X-RAY DIFFRACTION
3.59
65.72
VAPOR DIFFUSION, HANGING DROP
null
1.6 M sodium-potassium (L)-tartrate, 0.1 M Bis-Tris pH 6.5
291
2018-01-25
2018-05-30
6,228
2
786
238
null
90.11
2
2.2
experimental
null
0.2214
0.1903
Human Mtr4 helicase in complex with ZCCHC8-CTD
SGDTDEPIFGKKPRIEESITEDLSLADLMPRVKVQSVETVEGCTHEVALPAEEDYLPLKPRVGKAAKEYPFILDAFQREAIQCVDNNQSVLVSAHTSAGKTVCAEYAIALALREKQRVIFTSPIKALSNQKYREMYEEFQDVGLMTGDVTINPTASCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDSERGVVWEETIILLPDNVHYVFLSATIPNARQFAEWICHLHKQPCHVIYTDYRPTPLQHYIFPAGGDGLHLVVDENGDFREDNFNTAMQVLRDAGDLAKGDQKGRKGGTKGPSNVFKIVKMIMERNFQPVIIFSFSKKDCEAYALQMTKLDFNTDEEKKMVEEVFSNAIDCLSDEDKKLPQVEHVLPLLKRGIGIHHGGLLPILKETIEILFSEGLIKALFATETFAMGINMPARTVLFTNARKFDGKDFRWISSGEYIQMSGRAGRRGMDDRGIVILMVDEKMSPTIGKQLLKGSADPLNSAFHLTYNMVLNLLRVEEINPEYMLEKSFYQFQHYRAIPGSRTVLQMDELKCRKRVLRRLGFATSSDVIEMKGRVACEISSADELLLTEMMFNGLFNDLSAEQATALLSCFVFQENSSEMPKLTEQLAGPLRQMQECAKRIAKVSAEAKLEIDEETYLSSFKPHLMDVVYTWATGATFAHICKMTDVFEGSIIRCMRRLEELLRQMCQAAKAIGNTELENKFAEGITKIKRDIVFAASLYL
Protein
734
polypeptide(L)
1
83.206
Exosome RNA helicase MTR4,Exosome RNA helicase MTR4
3.6.4.13
PDB Primary Data
Homo sapiens
9,606
786
2
2
1
Hetero 2-mer
A1, B1
TLA
C4 H6 O6
150.087
L(+)-TARTARIC ACID
InChI=1S/C4H6O6/c5-1(3(7)8)2(6)4(9)10/h1-2,5-6H,(H,7,8)(H,9,10)/t1-,2-/m1/s1
C(C(C(=O)O)O)(C(=O)O)O
null
6,533
5MJ6
X-RAY DIFFRACTION
2.39
58.98
VAPOR DIFFUSION, SITTING DROP
8.5
18.8% (w/v) PEG of mean MW 20000, 37.6% (v/v) PEG monomethyl ether of mean MW 500, 50.2 mM Bicine, 43.8 mM Trizma base (pH of buffer mixture: 8.5) and 0.282 M each of the following halogens: Sodium fluoride, Sodium bromide and Sodium iodide
291
2016-11-30
2017-04-05
15,376
2
1,762
240
2
217.25
1
2.53
experimental
null
0.2292
0.1738
Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.
ATNGKLFPWAQIRLPTAVVPLRYELSLHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYHGQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVAFIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWWNDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQTLDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVTEGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINPYVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLEKLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAMKLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASSEDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGSYTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKSLTWWLRTETSQVAPA
Protein
881
polypeptide(L)
2
101.182
Leucyl-cystinyl aminopeptidase
3.4.11.3
PDB Primary Data
Homo sapiens
9,606
881
1
1
1
Monomer
A1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
7,663
6EPU
X-RAY DIFFRACTION
4.06
69.68
VAPOR DIFFUSION, HANGING DROP
5.5
2M (NH4)2SO4, 0.1M Bis-Tris pH 5.5
277
2017-10-12
2018-10-31
1,240
1
130
139
null
15.8
1
1.8
experimental
null
0.2184
0.192
The ATAD2 bromodomain in complex with compound 2
SMQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESR
Protein
130
polypeptide(L)
1
15.454
ATPase family AAA domain-containing protein 2
3.6.1.3
PDB Primary Data
Homo sapiens
9,606
130
1
1
1
Monomer
A1
SO4
O4 S
96.063
SULFATE ION
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
[O-]S(=O)(=O)[O-]
null
9,033
6O47
X-RAY DIFFRACTION
2.87
57.19
VAPOR DIFFUSION, HANGING DROP
7
0.064 M sodium citrate 7.0, 0.1 M HEPES, pH 7.0, 10% PEG5000MME
293
2019-02-28
2019-05-29
3,117
1
372
180
null
44.77
1
2.196
experimental
null
0.2214
0.1815
human cGAS core domain (K427E/K428E) bound with RU-521
SILVRRDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQLKERFKDEEHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
Protein
372
polypeptide(L)
1
43.486
Cyclic GMP-AMP synthase
2.7.7.86
PDB Primary Data
Homo sapiens
9,606
372
1
1
1
Monomer
A1
CIT
C6 H8 O7
192.124
CITRIC ACID
InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)
C(C(=O)O)C(CC(=O)O)(C(=O)O)O
null
8,108
7LFO
X-RAY DIFFRACTION
3.04
59.59
VAPOR DIFFUSION, HANGING DROP
7.5
140 g/L PEG8000, 100 mM HEPES, 200 mM magnesium acetate, pH 7.5
277.15
2021-01-18
2021-05-26
2,455
1
329
146
null
38.46
1
1.94
experimental
47.258
0.243
0.2004
Protein Tyrosine Phosphatase 1B
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNLEHHHHHH
Protein
329
polypeptide(L)
1
38.437
Tyrosine-protein phosphatase non-receptor type 1
3.1.3.48
PDB Primary Data
Homo sapiens
9,606
329
1
1
1
Monomer
A1
MG
Mg
24.305
MAGNESIUM ION
InChI=1S/Mg/q+2
[Mg+2]
null
5,836
8A2D
X-RAY DIFFRACTION
1.8
31.79
VAPOR DIFFUSION, SITTING DROP
6.5
20% PEG Smear High, 0.1M MES
293
2022-06-03
2022-10-19
2,770
1
326
387
null
38.27
1
1.11
experimental
15.73
0.1788
0.1632
EGFR kinase domain (L858R/V948R) in complex with 2-[4-(difluoromethyl)-6-[2-[4-[[4-(hydroxymethyl)-1-piperidyl]methyl]phenyl]ethynyl]-7-methyl-indazol-2-yl]-2-spiro[6,7-dihydropyrrolo[1,2-c]imidazole-5,1'-cyclopropane]-1-yl-N-thiazol-2-yl-acetamide
GSMNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGRAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
Protein
326
polypeptide(L)
1
37.327
Epidermal growth factor receptor
2.7.10.1
PDB Primary Data
Homo sapiens
9,606
326
1
1
1
Monomer
A1
EDO
C2 H6 O2
62.068
1,2-ETHANEDIOL
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
C(CO)O
null
11,536
5MPK
X-RAY DIFFRACTION
2.09
41.15
VAPOR DIFFUSION, HANGING DROP
7.5
0.1 M HEPES-Na, pH7.5, 0.2 M MgCl2, 25% P3350
277
2016-12-16
2018-01-17
2,022
2
238
127
null
29.32
1
1.9
experimental
null
0.2391
0.1828
Crystal structure of CREBBP bromodomain complexed with DK19
SMRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLG
Protein
119
polypeptide(L)
2
14.223
CREB-binding protein
2.3.1.48
PDB Primary Data
Homo sapiens
9,606
119
1
1
1
Monomer
A1
0BC
C21 H18 N6 O3 S
434.471
~{N}-(5-ethanoyl-2-ethoxy-phenyl)-3-(2~{H}-1,2,3,4-tetrazol-5-yl)-5-(1,3-thiazol-4-yl)benzamide
InChI=1S/C21H18N6O3S/c1-3-30-19-5-4-13(12(2)28)9-17(19)23-21(29)16-7-14(18-10-31-11-22-18)6-15(8-16)20-24-26-27-25-20/h4-11H,3H2,1-2H3,(H,23,29)(H,24,25,26,27)
CCOc1ccc(cc1NC(=O)c2cc(cc(c2)c3n[nH]nn3)c4cscn4)C(=O)C
null
10,605
7PNR
X-RAY DIFFRACTION
2.29
46.21
VAPOR DIFFUSION, SITTING DROP
null
Malic acid/NaOH pH 7.0, PEG 3350
289
2021-09-07
2021-09-29
1,020
1
121
59
3
13.85
1
1.6
experimental
27.906
0.20103
0.18981
Human Angiogenin mutant-S28AT36AS37A
QDNSRYTHFLTQHYDAKPQGRDDRYCEAIMRRRGLAAPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFR
Protein
121
polypeptide(L)
1
13.853
Angiogenin
3.1.27
PDB Primary Data
Homo sapiens
9,606
121
1
1
1
Monomer
A1
null
null
null
null
null
null
null
7,401
7U99
X-RAY DIFFRACTION
3.41
63.95
VAPOR DIFFUSION, HANGING DROP
6.5
0.1 M MES pH 6.5, 1.1 M Sodium Citrate
293
2022-03-10
2022-11-23
2,490
1
331
24
null
38.26
1
2.5
experimental
69.706
0.2139
0.187
EGFR kinase in complex with a macrocyclic inhibitor
GSTSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
Protein
331
polypeptide(L)
1
37.636
Epidermal growth factor receptor
2.7.10.1
PDB Primary Data
Homo sapiens
9,606
331
1
1
1
Monomer
A1
M0R
C21 H22 Cl N3 O5
431.869
19-chloro-22-methoxy-8,9,11,12,14,15-hexahydro-21H-4,6-ethenopyrimido[5,4-m][1,4,7,10,15]benzotetraoxazacycloheptadecine
InChI=1S/C21H22ClN3O5/c1-26-19-12-16-15-11-20(19)30-9-7-28-5-4-27-6-8-29-18-3-2-14(22)10-17(18)25-21(15)24-13-23-16/h2-3,10-13H,4-9H2,1H3,(H,23,24,25)
COc1cc2c3cc1OCCOCCOCCOc4ccc(cc4Nc3ncn2)Cl
Y
11,247
5QD3
X-RAY DIFFRACTION
3.16
61.08
hanging drop
null
CRYSTALS WERE GROWN AT 19C BY VAPOUR DIFFUSION IN HANGING DROPS FROM 1.0M AMMONIUM SULFATE IN WATER. PROTEIN STOCK WAS BACE MUT46B BATCH XVI 7.0MG/ML IN 10MM TRIS-HCL PH 7.4, 25MM NACL, WITH A 6-FOLD EXCESS OF BMC010 ADDED FROM A 50MM STOCK SOLUTION IN 90% DMSO-D6 (1.7% DMSO IN DROP). A SOLUTION CONTAINING 1.2M AMMONIUM SULFATE, 25% GLYCEROL, 1MM BMC010 AND 1.8% DMSO WAS USED AS CRYO-PROTECTANT.
292
2017-12-01
2020-06-03
9,374
3
1,206
353
9
135.9
1
2.46
experimental
47.78
0.2
0.164
Crystal structure of BACE complex with BMC010
GPDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNI
Protein
402
polypeptide(L)
3
44.777
Beta-secretase 1
3.4.23.46
PDB Primary Data
Homo sapiens
9,606
402
1
1
1
Monomer
A1
E6M
C32 H49 N3 O3
523.75
(10R,12S)-12-[(1R)-1-hydroxy-2-({[3-(propan-2-yl)phenyl]methyl}amino)ethyl]-17-(methoxymethyl)-10-methyl-2,13-diazabicyclo[13.3.1]nonadeca-1(19),15,17-trien-14-one
InChI=1S/C32H49N3O3/c1-23(2)27-13-10-12-25(16-27)20-33-21-31(36)30-15-24(3)11-8-6-5-7-9-14-34-29-18-26(22-38-4)17-28(19-29)32(37)35-30/h10,12-13,16-19,23-24,30-31,33-34,36H,5-9,11,14-15,20-22H2,1-4H3,(H,35,37)/t24-,30+,31-/m1/s1
CC1CCCCCCCNc2cc(cc(c2)C(=O)NC(C1)C(CNCc3cccc(c3)C(C)C)O)COC
null
2,907
8B78
X-RAY DIFFRACTION
2.75
55.23
VAPOR DIFFUSION, SITTING DROP
null
PEG 3350 LITHIUM SULFATE
293
2022-09-29
2023-07-12
1,524
1
168
124
null
20.11
1
1.11
experimental
20.835
0.2357
0.2236
KRasG12C ligand complex
GMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVDDAFYTLVREIRKHK
Protein
168
polypeptide(L)
1
19.195
GTPase KRas
3.6.5.2
PDB Primary Data
Homo sapiens
9,606
168
1
1
1
Monomer
A1
MG
Mg
24.305
MAGNESIUM ION
InChI=1S/Mg/q+2
[Mg+2]
null
8,522
8B6M
X-RAY DIFFRACTION
2.65
53.5
VAPOR DIFFUSION, SITTING DROP
8.5
100 mM Tris, 22% w/v PEG3350, 200 mM Li2SO4, 250 mM NaCl, 20% v/v glycerol
277.15
2022-09-27
2023-10-11
3,703
4
438
200
null
51.41
2
1.6
experimental
27.2
0.2194
0.1849
Tankyrase 2 in complex with an inhibitor
SMLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMK
Protein
171
polypeptide(L)
2
19.482
Poly [ADP-ribose] polymerase tankyrase-2
2.4.2.30
PDB Primary Data
Homo sapiens
9,606
219
2
2
1
Hetero 2-mer
A1, B1
OY6
C30 H27 N5 O4 S
553.631
~{N}-(2-methoxyphenyl)-4-[[2-(4-oxidanylidene-3~{H}-quinazolin-2-yl)ethyl-(thiophen-2-ylmethyl)carbamoyl]amino]benzamide
InChI=1S/C30H27N5O4S/c1-39-26-11-5-4-10-25(26)33-28(36)20-12-14-21(15-13-20)31-30(38)35(19-22-7-6-18-40-22)17-16-27-32-24-9-3-2-8-23(24)29(37)34-27/h2-15,18H,16-17,19H2,1H3,(H,31,38)(H,33,36)(H,32,34,37)
COc1ccccc1NC(=O)c2ccc(cc2)NC(=O)N(CCC3=Nc4ccccc4C(=O)N3)Cc5cccs5
Y
6,429
5NIA
X-RAY DIFFRACTION
2.46
50
VAPOR DIFFUSION, HANGING DROP
null
8% (w/v) PEG 20 000, 15% (w/v) PEG MME 550, 100 mM Hepes/MOPS pH 7.7-8.0, 15 mM CaCl2, 15 mM MgCl2
294
2017-03-23
2017-08-23
5,308
1
617
360
null
70.26
1
1.764
experimental
47.94
0.2074
0.1801
Crystal structure of human LTA4H mutant D375N in open conformation (crystal form I)
MHHHHHHPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPNVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
Protein
617
polypeptide(L)
1
70.192
Leukotriene A-4 hydrolase
3.3.2.6
PDB Primary Data
Homo sapiens
9,606
617
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
3,538
7A2H
X-RAY DIFFRACTION
2.67
53.88
VAPOR DIFFUSION, SITTING DROP
null
Reservoir composition: 28 % (w/v) PEG6000, 0.9 M LiCl, 0.1 M, Tris/HCl, pH 8.5; drop composition prior to equilibration: 0.01 ml reservoir solution + 0.02 ml CK2alpha' (mutant Cys336Ser)/inhibitor MB002 mixture (0.180 ml 6 mg/ml CK2alpha'Cys336Ser, 0.5 M NaCl, 25 mM Tris/HCl, pH 8.5, mixed and pre-equilibrated with 0.02 ml 10 mM MB002 in dimethyl sulfoxide); the initial inhibitor MB002 was replaced by the inhibitor 5,6,7-tribromo-1H-imidazo[4,5-b]pyridine by extensive crystal soaking.
293
2020-08-18
2020-12-09
3,304
1
364
433
null
43.42
1
1.01
experimental
17.38
0.1495
0.1426
Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in complex with the ATP-competitive inhibitor 5,6,7-tribromo-1H-imidazo[4,5-b]pyridine
MGSSHHHHHHSQDPMPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPSADNAVLSSGLTAAR
Protein
364
polypeptide(L)
1
42.88
Casein kinase II subunit alpha'
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
364
1
1
1
Monomer
A1
QX2
C6 H2 Br3 N3
355.812
5,6,7-tris(bromanyl)-1~{H}-imidazo[4,5-b]pyridine
InChI=1S/C6H2Br3N3/c7-2-3(8)5(9)12-6-4(2)10-1-11-6/h1H,(H,10,11,12)
c1[nH]c2c(c(c(nc2n1)Br)Br)Br
Y
2,133
6T7Q
X-RAY DIFFRACTION
2.18
43.67
VAPOR DIFFUSION, HANGING DROP
5
50 mM Di-Ammoniumhydrogen citrate pH 5.0: 15 mg/mL hAR, 5.2 mg/mL DTT, 0.7 mg/mL NADP+, 5% (w/v) PEG 6000 Reservoir: 120 mM Di-Ammoniumhydrogen citrate pH 5.0, 20% (w/v) PEG 6000 Soaking-buffer: 120 mM Di-Ammoniumhydrogen citrate pH 5.0, 25% (w/v) PEG 6000
291
2019-10-23
2020-11-18
3,233
1
316
409
null
37.14
1
1.01
experimental
11.81
0.1322
0.1177
Human Aldose Reductase Mutant L301A in Complex with a Ligand with an IDD Structure (3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid)
MASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALASCTSHKDYPFHEEF
Protein
316
polypeptide(L)
1
35.856
Aldo-keto reductase family 1 member B1
1.1.1.300
PDB Primary Data
Homo sapiens
9,606
316
1
1
1
Monomer
A1
4G7
C17 H14 F N O6
347.295
3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid
InChI=1S/C17H14FNO6/c18-12-4-5-13(14(7-12)25-9-15(20)21)16(22)19-8-10-2-1-3-11(6-10)17(23)24/h1-7H,8-9H2,(H,19,22)(H,20,21)(H,23,24)
c1cc(cc(c1)C(=O)O)CNC(=O)c2ccc(cc2OCC(=O)O)F
Y
1,897
5RW3
X-RAY DIFFRACTION
2.11
41.62
VAPOR DIFFUSION, SITTING DROP
6.5
30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulfate, 100 mM MES/imidazole, pH 6.5, 20% PEG500 MME, 10% PEG20000
293
2020-10-30
2020-11-11
4,745
1
463
442
null
53.35
1
1.37
experimental
18.421
0.196
0.1707
INPP5D PanDDA analysis group deposition -- Crystal Structure of the phosphatase and C2 domains of SHIP1 in complex with Z2064898339
SMEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQ
Protein
463
polypeptide(L)
1
52.878
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
3.1.3.86
PDB Primary Data
Homo sapiens
9,606
463
1
1
1
Monomer
A1
WLY
C14 H19 N O2
233.306
2-(4-methylphenyl)-N-{[(2S)-oxolan-2-yl]methyl}acetamide
InChI=1S/C14H19NO2/c1-11-4-6-12(7-5-11)9-14(16)15-10-13-3-2-8-17-13/h4-7,13H,2-3,8-10H2,1H3,(H,15,16)/t13-/m0/s1
Cc1ccc(cc1)CC(=O)NCC2CCCO2
null
8,188
8FPW
X-RAY DIFFRACTION
2.31
46.85
VAPOR DIFFUSION, HANGING DROP
8
20-24% PEG8K, 15% Dioxane, 0.1M Tris pH8.0
277
2023-01-05
2024-06-05
1,756
1
183
231
null
21.25
1
1.4
experimental
null
0.2079
0.1781
Crystal structure of tumor related RhoA mutant A161V in complex with GDP
GSMAAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSVKTKDGVREVFEMATRAALQA
Protein
183
polypeptide(L)
1
20.607
Transforming protein RhoA
3.6.5.2
PDB Primary Data
Homo sapiens
9,606
183
1
1
1
Monomer
A1
MG
Mg
24.305
MAGNESIUM ION
InChI=1S/Mg/q+2
[Mg+2]
Y
11,438
6FCK
X-RAY DIFFRACTION
2.42
49.1
VAPOR DIFFUSION, HANGING DROP
null
16% Peg8k, 0.1M Caco pH 6.8, 0.15M AS
298
2017-12-20
2018-01-17
2,554
1
276
331
null
32.27
1
1.9
experimental
21.7
0.214
0.174
CHK1 KINASE IN COMPLEX WITH COMPOUND 13
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRP
Protein
276
polypeptide(L)
1
31.841
Serine/threonine-protein kinase Chk1
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
276
1
1
1
Monomer
A1
D4Z
C20 H22 N4 O
334.415
2-phenyl-4-[[(3~{S})-piperidin-3-yl]amino]-1~{H}-indole-7-carboxamide
InChI=1S/C20H22N4O/c21-20(25)15-8-9-17(23-14-7-4-10-22-12-14)16-11-18(24-19(15)16)13-5-2-1-3-6-13/h1-3,5-6,8-9,11,14,22-24H,4,7,10,12H2,(H2,21,25)/t14-/m0/s1
c1ccc(cc1)c2cc3c(ccc(c3[nH]2)C(=O)N)NC4CCCNC4
Y
8,713
5OYF
X-RAY DIFFRACTION
1.98
37.81
VAPOR DIFFUSION, HANGING DROP
6.5
112.5mM Mes pH 6.5, 35% glycerol ethoxylate, 180 mM ammonium acetate
298
2017-09-08
2018-02-28
3,086
1
342
201
null
41.64
1
1.54
experimental
30.35
0.216
0.185
The crystal structure of CK2alpha in complex with compound 31
SGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVAAAKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKREAMEHPYFYTVVK
Protein
342
polypeptide(L)
1
40.786
Casein kinase II subunit alpha
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
342
1
1
1
Monomer
A1
B4Q
C25 H27 N3
369.502
2-(1~{H}-benzimidazol-2-yl)-~{N}-[[4-(2-ethylphenyl)-3-methyl-phenyl]methyl]ethanamine
InChI=1S/C25H27N3/c1-3-20-8-4-5-9-22(20)21-13-12-19(16-18(21)2)17-26-15-14-25-27-23-10-6-7-11-24(23)28-25/h4-13,16,26H,3,14-15,17H2,1-2H3,(H,27,28)
CCc1ccccc1c2ccc(cc2C)CNCCc3[nH]c4ccccc4n3
Y
5,180
6YVY
X-RAY DIFFRACTION
2.82
56.34
VAPOR DIFFUSION, HANGING DROP
7.5
15% PEG 3350
294
2020-04-28
2021-02-10
9,023
4
1,128
507
4
131.15
1
1.918
experimental
39.24
0.2353
0.2141
FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH 4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide
GSGSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEE
Protein
282
polypeptide(L)
4
32.304
Focal adhesion kinase 1
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
282
1
1
1
Monomer
A1
P1E
C19 H25 F3 N6 O2 S
458.501
4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide
InChI=1S/C19H25F3N6O2S/c1-23-31(29,30)13-9-7-12(8-10-13)25-18-24-11-14(19(20,21)22)17(27-18)26-15-5-4-6-16(15)28(2)3/h7-11,15-16,23H,4-6H2,1-3H3,(H2,24,25,26,27)/t15-,16-/m1/s1
CNS(=O)(=O)c1ccc(cc1)Nc2ncc(c(n2)NC3CCCC3N(C)C)C(F)(F)F
Y
9,174
5VUB
X-RAY DIFFRACTION
3.27
62.43
VAPOR DIFFUSION, HANGING DROP
5.5
100MM CITRATE BUFFER, PH 5.5, 200MM NACL, 1M NH4HPO4
293
2017-05-18
2017-12-13
2,501
1
298
238
null
34.69
1
2.0
experimental
32.39
0.1837
0.1603
Pim1 Kinase in complex with a benzofuranone inhibitor
MKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSKSGPSSGENLYFQ
Protein
298
polypeptide(L)
1
34.204
Serine/threonine-protein kinase pim-1
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
298
1
1
1
Monomer
A1
GOL
C3 H8 O3
92.094
GLYCEROL
InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
C(C(CO)O)O
null
8,067
5NK9
X-RAY DIFFRACTION
1.96
37.36
VAPOR DIFFUSION, SITTING DROP
6.5
37.5% MPD/PEG1000/PEG3350 (MD), 0.1 M Amino Acids Mix (MD), 0.1 M Hepes pH6.5
291
2017-03-31
2017-06-07
2,653
1
306
261
null
34.96
1
1.588
experimental
null
0.1945
0.1621
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2e
GDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSG
Protein
306
polypeptide(L)
1
34.463
Ephrin type-A receptor 2
2.7.10.1
PDB Primary Data
Homo sapiens
9,606
306
1
1
1
Monomer
A1
912
C25 H29 Cl N4 O3 S
501.041
(2~{Z})-~{N}-(2-chloranyl-6-methyl-phenyl)-2-[3-[(4-methyl-4-oxidanyl-cyclohexyl)carbamoyl]phenyl]imino-1,3-thiazolidine-5-carboxamide
InChI=1S/C25H29ClN4O3S/c1-15-5-3-8-19(26)21(15)30-23(32)20-14-27-24(34-20)29-18-7-4-6-16(13-18)22(31)28-17-9-11-25(2,33)12-10-17/h3-8,13,17,20,33H,9-12,14H2,1-2H3,(H,27,29)(H,28,31)(H,30,32)/t17-,20-,25-/m1/s1
Cc1cccc(c1NC(=O)C2CNC(=Nc3cccc(c3)C(=O)NC4CCC(CC4)(C)O)S2)Cl
null
7,746
5EHV
X-RAY DIFFRACTION
2.08
40.81
VAPOR DIFFUSION, SITTING DROP
null
ammonium sulfate, tris-chloride
280
2015-10-29
2016-03-09
2,578
1
260
382
null
29.83
1
1.208
experimental
null
0.1746
0.1532
human carbonic anhydrase II in complex with ligand
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
260
polypeptide(L)
1
29.289
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
260
1
1
1
Monomer
A1
5ON
C18 H16 O5
312.317
(~{E})-3-[3-[[3-(2-hydroxy-2-oxoethyl)phenyl]methoxy]phenyl]prop-2-enoic acid
InChI=1S/C18H16O5/c19-17(20)8-7-13-3-2-6-16(10-13)23-12-15-5-1-4-14(9-15)11-18(21)22/h1-10H,11-12H2,(H,19,20)(H,21,22)/b8-7+
c1cc(cc(c1)COc2cccc(c2)C=CC(=O)O)CC(=O)O
null
1,817
5VLR
X-RAY DIFFRACTION
2.6
53.2
VAPOR DIFFUSION
null
NULL, VAPOR DIFFUSION, TEMPERATURE 293K
300
2017-04-26
2017-06-07
8,448
2
1,183
24
null
137.48
2
2.8
experimental
87.32
0.279
0.208
CRYSTAL STRUCTURE OF PI3K DELTA IN COMPLEX WITH A TRIFLUORO-ETHYL-PYRAZOL-PYROLOTRIAZINE INHIBITOR
NQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKT
Protein
1,013
polypeptide(L)
1
115.959
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
2.7.1.153
PDB Primary Data
Homo sapiens
9,606
1,013
1
1
1
Monomer
A1
9EM
C25 H25 F3 N8 O2
526.514
4-acetyl-1-(3-{4-amino-5-[1-(2,2,2-trifluoroethyl)-1H-pyrazol-5-yl]pyrrolo[2,1-f][1,2,4]triazin-7-yl}phenyl)-3,3-dimethylpiperazin-2-one
InChI=1S/C25H25F3N8O2/c1-15(37)34-10-9-33(23(38)24(34,2)3)17-6-4-5-16(11-17)20-12-18(21-22(29)30-14-32-36(20)21)19-7-8-31-35(19)13-25(26,27)28/h4-8,11-12,14H,9-10,13H2,1-3H3,(H2,29,30,32)
CC(=O)N1CCN(C(=O)C1(C)C)c2cccc(c2)c3cc(c4n3ncnc4N)c5ccnn5CC(F)(F)F
null
11,551
5R56
X-RAY DIFFRACTION
2.01
38.94
VAPOR DIFFUSION, SITTING DROP
7.5
0.1M HEPES pH 7.5, 0.3M sodium/potassium phosphate, 15% PEG Smear High, 20% ethylene glycol
277
2020-02-28
2020-07-01
2,458
1
304
163
null
33.43
1
1.51
experimental
24.013
0.2156
0.1839
PanDDA analysis group deposition -- Crystal Structure of human NUDT22 in complex with N13688a
SMDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVRRLPETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
Protein
304
polypeptide(L)
1
32.707
Uridine diphosphate glucose pyrophosphatase NUDT22
3.6.1.45
PDB Primary Data
Homo sapiens
9,606
304
1
1
1
Monomer
A1
S07
C14 H19 N O3
249.306
2-(2,4-dimethylphenoxy)-1-morpholin-4-yl-ethanone
InChI=1S/C14H19NO3/c1-11-3-4-13(12(2)9-11)18-10-14(16)15-5-7-17-8-6-15/h3-4,9H,5-8,10H2,1-2H3
Cc1ccc(c(c1)C)OCC(=O)N2CCOCC2
null
1,937
4YXO
X-RAY DIFFRACTION
2.08
40.75
VAPOR DIFFUSION, HANGING DROP
7.8
2.5 uL of the protein solution (10 mg/ml hCAII in 50 mM Tris pH 7.8) were mixed with 2.5 uL of the well solution (2.7 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with p-chloromercurybenzoicacid) and placed as a hanging drop. Crystals appeared after several days. The crystals were soaked in 3.0 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with the inhibitor, for 1 day.
291
2015-03-23
2016-02-03
2,362
1
260
239
null
30.14
1
1.06
experimental
null
0.164
0.1486
Human Carbonic Anhydrase II complexed with an inhibitor with a benzenesulfonamide group (3).
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
260
polypeptide(L)
1
29.289
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
260
1
1
1
Monomer
A1
MBO
C7 H5 Hg O2
321.703
MERCURIBENZOIC ACID
InChI=1S/C7H5O2.Hg/c8-7(9)6-4-2-1-3-5-6;/h2-5H,(H,8,9);
c1cc(ccc1C(=O)O)[Hg]
null
337
7U4I
X-RAY DIFFRACTION
2.18
43.47
MICROBATCH
7
0.2 M potassium thiocyanate and 20% (w/v) PEG 3350
291
2022-02-28
2022-12-07
2,811
2
384
179
null
44.32
1
1.97
experimental
31.7419
0.2458
0.2007
Crystal structure of human GPX4-U46C-R152H in complex with CDS9
MGSSHHHHHHSSGLVPRGSHMLEAASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKHYGPMEEPLVIEKDLPHYF
Protein
192
polypeptide(L)
2
21.869
Phospholipid hydroperoxide glutathione peroxidase
1.11.1.12
PDB Primary Data
Homo sapiens
9,606
192
1
1
1
Monomer
A1
L9U
C7 H8 Br N O S
234.114
2-bromo-N-[(thiophen-2-yl)methyl]acetamide
InChI=1S/C7H8BrNOS/c8-4-7(10)9-5-6-2-1-3-11-6/h1-3H,4-5H2,(H,9,10)
c1cc(sc1)CNC(=O)CBr
null
2,335
5KW2
X-RAY DIFFRACTION
3.12
60.54
LIPIDIC CUBIC PHASE
null
0.1 M Tris HCl, pH 8.5, 30% PEG 400, 0.2 M ammonium formate.
298
2016-07-15
2018-05-02
3,237
1
491
52
1
53.73
1
2.76
experimental
41.374
0.2727
0.2304
The extra-helical binding site of GPR40 and the structural basis for allosteric agonism and incretin stimulation
MDYKDDDDKGSATMDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSAVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFAPLYAGGGFLAALSAARYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCFVGCLRALARGSNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYGSLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQKAENLYFQGHHHHHHHH
Protein
491
polypeptide(L)
1
53.102
Free fatty acid receptor 1,Lysozyme,Free fatty acid receptor 1
3.2.1.17
PDB Primary Data
Homo sapiens
9,606
491
1
1
1
Monomer
A1
6XQ
C38 H45 N3 O5
623.781
(3~{S})-3-cyclopropyl-3-[2-[1-[2-[2,2-dimethylpropyl-(6-methylpyridin-2-yl)carbamoyl]-5-methoxy-phenyl]piperidin-4-yl]-1-benzofuran-6-yl]propanoic acid
InChI=1S/C38H45N3O5/c1-24-7-6-8-35(39-24)41(23-38(2,3)4)37(44)30-14-13-29(45-5)21-32(30)40-17-15-26(16-18-40)33-20-28-12-11-27(19-34(28)46-33)31(22-36(42)43)25-9-10-25/h6-8,11-14,19-21,25-26,31H,9-10,15-18,22-23H2,1-5H3,(H,42,43)/t31-/m0/s1
Cc1cccc(n1)N(CC(C)(C)C)C(=O)c2ccc(cc2N3CCC(CC3)c4cc5ccc(cc5o4)C(CC(=O)O)C6CC6)OC
null
4,395
5SKJ
X-RAY DIFFRACTION
2.6
52.74
VAPOR DIFFUSION, SITTING DROP
7.5
5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2
295
2022-02-01
2022-10-12
10,527
4
1,372
277
4
159.22
1
2.74
experimental
45.162
0.2489
0.166
Crystal Structure of human phosphodiesterase 10 in complex with 6-cyclopropyl-N-[2-[2-(methylamino)-2-oxoethyl]phenyl]-3-(pyrimidin-5-ylamino)pyridine-2-carboxamide
GSSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Protein
343
polypeptide(L)
4
39.413
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
3.1.4.17
PDB Primary Data
Homo sapiens
9,606
343
1
1
1
Monomer
A1
KG3
C22 H22 N6 O2
402.449
6-cyclopropyl-N-{2-[2-(methylamino)-2-oxoethyl]phenyl}-3-[(pyrimidin-5-yl)amino]pyridine-2-carboxamide
InChI=1S/C22H22N6O2/c1-23-20(29)10-15-4-2-3-5-17(15)28-22(30)21-19(26-16-11-24-13-25-12-16)9-8-18(27-21)14-6-7-14/h2-5,8-9,11-14,26H,6-7,10H2,1H3,(H,23,29)(H,28,30)
CNC(=O)Cc1ccccc1NC(=O)c2c(ccc(n2)C3CC3)Nc4cncnc4
Y
2,072
8T2H
X-RAY DIFFRACTION
2.27
45.86
VAPOR DIFFUSION, HANGING DROP
6
1.8 M sodium malonate, 1.3% PEG 400
298
2023-06-06
2024-05-15
6,053
2
730
354
null
86.18
1
1.85
experimental
21.451
0.21303
0.16329
DYRK1A complex with DYR530
DSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTS
Protein
365
polypeptide(L)
2
42.439
Dual specificity tyrosine-phosphorylation-regulated kinase 1A
2.7.11.23
PDB Primary Data
Homo sapiens
9,606
365
1
1
1
Monomer
A1
XIR
C23 H24 F N7
417.482
(4P)-4-{(3M)-3-[3-fluoro-4-(4-methylpiperazin-1-yl)phenyl]-2-methyl-3H-imidazo[4,5-b]pyridin-5-yl}pyridin-2-amine
InChI=1S/C23H24FN7/c1-15-27-20-5-4-19(16-7-8-26-22(25)13-16)28-23(20)31(15)17-3-6-21(18(24)14-17)30-11-9-29(2)10-12-30/h3-8,13-14H,9-12H2,1-2H3,(H2,25,26)
Cc1nc2ccc(nc2n1c3ccc(c(c3)F)N4CCN(CC4)C)c5ccnc(c5)N
Y
8,639
7RNY
X-RAY DIFFRACTION
2.09
41.06
VAPOR DIFFUSION, HANGING DROP
7.8
1.6 M sodium citrate, 50 mM tris base
293
2021-07-30
2022-06-08
2,323
1
260
215
null
29.77
1
1.29
experimental
12.871
0.174
0.154
Carbonic Anhydrase II in complex with 3-ureido benzenesulfonamide derivative
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
260
polypeptide(L)
1
29.289
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
260
1
1
1
Monomer
A1
65M
C15 H17 N3 O3 S
319.379
3-{[benzyl(methyl)carbamoyl]amino}benzene-1-sulfonamide
InChI=1S/C15H17N3O3S/c1-18(11-12-6-3-2-4-7-12)15(19)17-13-8-5-9-14(10-13)22(16,20)21/h2-10H,11H2,1H3,(H,17,19)(H2,16,20,21)
CN(Cc1ccccc1)C(=O)Nc2cccc(c2)S(=O)(=O)N
Y
1,726
5CLS
X-RAY DIFFRACTION
2.74
55.08
VAPOR DIFFUSION, SITTING DROP
5.4
Na Citrate, Tert-butanol
292
2015-07-16
2016-01-13
3,351
1
371
329
1
42.51
1
1.75
experimental
22.373
0.18885
0.16001
Structure of human methionine aminopeptidase-2 complexed with spiroepoxytriazole inhibitor (+)-31a
GPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Protein
371
polypeptide(L)
1
41.51
Methionine aminopeptidase 2
3.4.11.18
PDB Primary Data
Homo sapiens
9,606
371
1
1
1
Monomer
A1
DMS
C2 H6 O S
78.133
DIMETHYL SULFOXIDE
InChI=1S/C2H6OS/c1-4(2)3/h1-2H3
CS(=O)C
null
8,331
5FDC
X-RAY DIFFRACTION
2.08
40.81
VAPOR DIFFUSION, HANGING DROP
null
2.5 M ammonium sulphate, 0.3 M sodium chloride, 0.1 M Tris-HCl, pH 8.4 and 5 mM 4-(hydroxymercurybenzoate)
293
2015-12-16
2016-05-18
2,384
1
260
264
null
30.03
1
1.75
experimental
null
0.204
0.17
Crystal structure of Human Carbonic Anhydrase II in complex with the anticonvulsant sulfamide JNJ-26990990 and its S,S-dioxide analog.
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
260
polypeptide(L)
1
29.289
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
260
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
1,047
5LAB
X-RAY DIFFRACTION
2.26
45.26
VAPOR DIFFUSION, SITTING DROP
8
Tris, PEG6000, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
293
2016-06-14
2016-08-10
1,508
1
159
236
null
18.18
1
1.34
experimental
21.754
0.1945
0.15515
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
Protein
159
polypeptide(L)
1
17.616
Macrophage metalloelastase
3.4.24.65
PDB Primary Data
Homo sapiens
9,606
159
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
7,706
4YYP
X-RAY DIFFRACTION
3.68
66.64
VAPOR DIFFUSION, SITTING DROP
null
Thin needles grew in precipitant solution containing 100 mM Hepes, pH 7.0, 20 mM MgCl2 and 22% Poly(acrylic acid sodium salt) 5100. After extensive optimization and seeding plate-like crystals were grown in a drop consisting of 50% PLK4-PB3/STIL-CC complex solution, 33.3% precipitant solution (100 mM phosphate/citrate pH 4.2, 40% (v/v) Ethanol, 5% (w/v) PEG 1000) and 16.7% of seed stock solution.
291
2015-03-24
2015-07-29
967
2
119
15
null
13.45
2
2.6
experimental
89.61
0.2542
0.2174
Crystal structure of human PLK4-PB3 in complex with STIL-CC
SAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH
Protein
87
polypeptide(L)
1
9.573
Serine/threonine-protein kinase PLK4
2.7.11.21
PDB Primary Data
Homo sapiens
9,606
119
2
2
1
Hetero 2-mer
A1, B1
CL
Cl
35.453
CHLORIDE ION
InChI=1S/ClH/h1H/p-1
[Cl-]
null
7,563
8Q69
X-RAY DIFFRACTION
2.12
41.9
VAPOR DIFFUSION, SITTING DROP
6.5
0.1 M MES pH 6.3-6.9, 50 mM Na2SO4, 18-25 % PEG 6000
290
2023-08-11
2024-08-21
4,919
2
552
405
null
66.81
1
1.96
experimental
null
0.2892
0.2423
Crystal structure of HsRNMT complexed with inhibitor DDD1060606
SQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMGLGCLSKSEWEATSIYLVFAFEKQQ
Protein
276
polypeptide(L)
2
32.551
mRNA cap guanine-N7 methyltransferase
2.1.1.56
PDB Primary Data
Homo sapiens
9,606
276
1
1
1
Monomer
A1
SAH
C14 H20 N6 O5 S
384.411
S-ADENOSYL-L-HOMOCYSTEINE
InChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
Y
2,815
6BH3
X-RAY DIFFRACTION
2.24
45.17
VAPOR DIFFUSION, SITTING DROP
null
1.2-1.35 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.6-9.2), 0-20% glycerol, 25 mM (Na/K) dibasic/monobasic phosphate
289
2017-10-29
2018-03-28
2,654
1
330
226
null
38.86
1
1.701
experimental
null
0.2157
0.1947
LINKED KDM5A JMJ DOMAIN BOUND TO THE INHIBITOR (S)-N-(1-(3-isopropyl-1H-pyrazole-5-carbonyl)pyrrolidin-3-yl)cyclopropanecarboxamide (Compound N55)
HNMAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRPREAFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCT
Protein
330
polypeptide(L)
1
37.945
Lysine-specific demethylase 5A, linked KDM5A JMJ domain
1.14.11
PDB Primary Data
Homo sapiens
9,606
330
1
1
1
Monomer
A1
DQJ
C15 H22 N4 O2
290.361
N-{(3S)-1-[5-(propan-2-yl)-1H-pyrazole-3-carbonyl]pyrrolidin-3-yl}cyclopropanecarboxamide
InChI=1S/C15H22N4O2/c1-9(2)12-7-13(18-17-12)15(21)19-6-5-11(8-19)16-14(20)10-3-4-10/h7,9-11H,3-6,8H2,1-2H3,(H,16,20)(H,17,18)/t11-/m0/s1
CC(C)c1cc(n[nH]1)C(=O)N2CCC(C2)NC(=O)C3CC3
Y
8,161
5OS0
X-RAY DIFFRACTION
2.79
55.84
VAPOR DIFFUSION, SITTING DROP
8.5
0.1 M Tris, pH 8.5: 0.5 M NaCl: 0.2 M MgCl2: 32.5 % v/v PEG 3350
298
2017-08-16
2017-11-01
2,333
1
265
141
null
31.51
1
1.74
experimental
43.1512
0.2635
0.2173
Crystal structure of Aurora-A kinase in complex with an allosterically binding fragment
QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLAGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPS
Protein
265
polypeptide(L)
1
30.798
Aurora kinase A
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
265
1
1
1
Monomer
A1
MG
Mg
24.305
MAGNESIUM ION
InChI=1S/Mg/q+2
[Mg+2]
null
9,936
4WZX
X-RAY DIFFRACTION
2.19
43.83
VAPOR DIFFUSION, SITTING DROP
6.5
50mM MES pH 6.5, 5mM Cobalt chloride, 800mM ammonium sulfate
295
2014-11-20
2015-06-03
896
2
118
69
null
13.44
2
1.3859
experimental
null
0.18
0.1513
ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins
GPHMGTSARDLLREMARDKPRLLAALEVASAAMAKEEAAGGEQDALDLYQHSLGELLLLLAAEPPGRRRELLHTEVQNLMARAEYLKEQVKMRES
Protein
95
polypeptide(L)
1
10.551
Serine/threonine-protein kinase ULK3
2.7.11.1
PDB Primary Data
Homo sapiens
9,606
118
2
2
1
Hetero 2-mer
A1, B1
CO
Co
58.933
COBALT (II) ION
InChI=1S/Co/q+2
[Co+2]
null
2,320
5RYC
X-RAY DIFFRACTION
2.1
41.44
VAPOR DIFFUSION, SITTING DROP
6.5
30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulfate, 100 mM MES/imidazole, pH 6.5, 20% PEG500 MME, 10% PEG20000
293
2020-10-30
2020-11-11
4,790
1
463
441
null
53.28
1
1.56
experimental
18.459
0.2051
0.174
INPP5D PanDDA analysis group deposition -- Crystal Structure of the phosphatase and C2 domains of SHIP1 in complex with Z18197050
SMEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQ
Protein
463
polypeptide(L)
1
52.878
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
3.1.3.86
PDB Primary Data
Homo sapiens
9,606
463
1
1
1
Monomer
A1
WL1
C8 H8 O2 S
168.213
methyl 4-sulfanylbenzoate
InChI=1S/C8H8O2S/c1-10-8(9)6-2-4-7(11)5-3-6/h2-5,11H,1H3
COC(=O)c1ccc(cc1)S
null
8,268
6HWO
X-RAY DIFFRACTION
2.62
53.1
VAPOR DIFFUSION, HANGING DROP
7.5
24% PEG 3350, 30% Ethylene Glycol, 0.1 M HEPES pH 7.5
293
2018-10-12
2019-07-24
11,546
4
1,456
590
null
174.3
1
1.99
experimental
43.247
0.25539
0.19819
Crystal structure of human phosphodiesterase 4D2 catalytic domain with inhibitor NPD-1335
GSHMIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTL
Protein
364
polypeptide(L)
4
41.808
cAMP-specific 3',5'-cyclic phosphodiesterase 4D
3.1.4.53
PDB Primary Data
Homo sapiens
9,606
364
1
1
1
Monomer
A1
PEG
C4 H10 O3
106.12
DI(HYDROXYETHYL)ETHER
InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2
C(COCCO)O
null
9,696
8YGZ
X-RAY DIFFRACTION
2.5
50.83
VAPOR DIFFUSION, SITTING DROP
null
0.2M Li2SO4, 0.1M Tris-HCl pH8.5, 30% PEG4,000
293
2024-02-27
2024-03-13
2,542
1
314
176
null
36.31
1
2.1
experimental
44.21
0.254
0.1949
The Crystal Structure of TGF beta R2 kinase domain from Biortus.
GHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLASAMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVASMADNVLADAGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSG
Protein
314
polypeptide(L)
1
35.587
TGF-beta receptor type-2
2.7.11.30
PDB Primary Data
Homo sapiens
9,606
314
1
1
1
Monomer
A1
EDO
C2 H6 O2
62.068
1,2-ETHANEDIOL
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
C(CO)O
Y
11,565
4XQ8
X-RAY DIFFRACTION
2.58
52.27
VAPOR DIFFUSION
null
0.1 M Lithium Sulfate monohydrate, 0.1 M HEPES-Sodium, 0.1 M Potassium Sodium Tartrate
277
2015-01-19
2016-02-24
4,236
4
680
99
1
78.83
1
2.798
experimental
null
0.2399
0.1817
Human DNA polymerase lambda- MgdATP binary complex and complex with 6 paired DNA
AQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
Protein
334
polypeptide(L)
2
37.349
DNA polymerase lambda
2.7.7.7
PDB Primary Data
Homo sapiens
9,606
346
3
3
1
Monomer
A1
DTP
C10 H16 N5 O12 P3
491.182
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
c1nc(c2c(n1)n(cn2)C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)N
null
3,386
6TUH
X-RAY DIFFRACTION
2.23
44.92
VAPOR DIFFUSION, SITTING DROP
8.5
0.1 M TRIS 8.5 pH, 32.5% w/v PEG 3350, 200mM MgCl2
298
2020-01-07
2020-11-25
5,181
4
676
80
2
80.98
1
2.25
experimental
71.72
0.276
0.236
The PH domain of Bruton's tyrosine kinase mutant R28C
AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPSFWIDGQYLCCSQTAKNAMGCQILEN
Protein
169
polypeptide(L)
4
19.967
Tyrosine-protein kinase BTK
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
169
1
1
1
Monomer
A1
NXT
C9 H10 O3
166.174
4,5,6,7-tetrahydro-1-benzofuran-3-carboxylic acid
InChI=1S/C9H10O3/c10-9(11)7-5-12-8-4-2-1-3-6(7)8/h5H,1-4H2,(H,10,11)
c1c(c2c(o1)CCCC2)C(=O)O
Y
10,375
4WMA
X-RAY DIFFRACTION
2.46
50.03
VAPOR DIFFUSION, HANGING DROP
6.5
0.2 M Li2SO4, 0.1 M Bis-Tris, and 21% PEG3350
293
2014-10-08
2015-09-30
2,905
2
356
135
5
42.04
2
1.62
experimental
31.982
0.24252
0.21914
Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with manganese,acceptor ligand and UDP-Glucose
SLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEASREVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFLSVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQFRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGHLGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCNTPIPED
Protein
306
polypeptide(L)
1
35.295
Xyloside xylosyltransferase 1
2.4.2
PDB Primary Data
Mus musculus
10,090
356
2
2
1
Hetero 2-mer
A1, B1
MN
Mn
54.938
MANGANESE (II) ION
InChI=1S/Mn/q+2
[Mn+2]
null
766
5OVX
X-RAY DIFFRACTION
2.53
51.29
VAPOR DIFFUSION, HANGING DROP
null
26-28% PEG3350, 0.1M Bis-Tris pH5.5, 0.2M Lithium sulfate
277
2017-08-30
2017-11-22
2,617
1
305
252
null
35.66
1
2.1
experimental
27.5
0.228
0.1954
X-Ray Characterization of Striatal-Enriched Protein Tyrosine Phosphatase Inhibitors
MHHHHHHSSGVDLGTENLYFQSMSRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSHQS
Protein
305
polypeptide(L)
1
35.221
Tyrosine-protein phosphatase non-receptor type 5
3.1.3.48
PDB Primary Data
Homo sapiens
9,606
305
1
1
1
Monomer
A1
AY5
C20 H17 Cl2 O5 P
439.226
[(~{S})-[4-[3-[(~{S})-(3,4-dichlorophenyl)-oxidanyl-methyl]phenyl]phenyl]-oxidanyl-methyl]phosphonic acid
InChI=1S/C20H17Cl2O5P/c21-17-9-8-16(11-18(17)22)19(23)15-3-1-2-14(10-15)12-4-6-13(7-5-12)20(24)28(25,26)27/h1-11,19-20,23-24H,(H2,25,26,27)/t19-,20-/m0/s1
c1cc(cc(c1)C(c2ccc(c(c2)Cl)Cl)O)c3ccc(cc3)C(O)P(=O)(O)O
null
2,861
6I0B
X-RAY DIFFRACTION
3.1
60.38
VAPOR DIFFUSION, HANGING DROP
null
MES pH 6.5 Ammonium Sulphate
293
2018-10-25
2019-03-27
4,566
1
529
114
3
63.29
1
2.384
experimental
null
0.2439
0.1892
Human butyrylcholinesterase in complex with the S enantiomer of a chlorotacrine-tryptophan multi-target inhibitor.
EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNPQETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV
Protein
529
polypeptide(L)
1
59.714
Cholinesterase
3.1.1.8
PDB Primary Data
Homo sapiens
9,606
529
1
1
1
Monomer
A1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
5,860
8I1J
X-RAY DIFFRACTION
1.83
32.82
VAPOR DIFFUSION, HANGING DROP
null
sodium citrate, caps, NaCl
293
2023-01-13
2023-03-22
3,186
2
312
334
1
37.19
1
1.08
experimental
20.24
0.1742
0.1418
Crystal structure of human MTH1(G2K/D120N mutant) in complex with 2-oxo-dATP at pH 9.7
MKASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDNSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV
Protein
156
polypeptide(L)
2
18.043
7,8-dihydro-8-oxoguanine triphosphatase
3.6.1.55
PDB Primary Data
Homo sapiens
9,606
156
1
1
1
Monomer
A1
6U4
C10 H16 N5 O13 P3
507.181
[[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate
InChI=1S/C10H16N5O13P3/c11-8-7-9(14-10(17)13-8)15(3-12-7)6-1-4(16)5(26-6)2-25-30(21,22)28-31(23,24)27-29(18,19)20/h3-6,16H,1-2H2,(H,21,22)(H,23,24)(H2,18,19,20)(H3,11,13,14,17)/t4-,5+,6+/m0/s1
C1C(C(OC1N2C=NC3=C(NC(=O)N=C32)N)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O
Y
3,844
7SUY
X-RAY DIFFRACTION
2.1
41.52
VAPOR DIFFUSION, HANGING DROP
7.8
1.6 M sodium citrate, 50 mM tris base
293
2021-11-18
2022-04-06
2,284
1
257
198
null
29.37
1
1.405
experimental
19.3444
0.1873
0.1653
Carbonic Anhydrase IX-mimic Complexed with 2-((3-Aminopropyl)(phenethyl)amino)-N-(4-fluorobenzyl)-N-(4-sulfamoylphenethyl)acetamide
HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVTFDDSQDKAVLKGGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTEGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
257
polypeptide(L)
1
28.844
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
257
1
1
1
Monomer
A1
C97
C15 H19 N3 O4 S
337.394
N-[(furan-2-yl)methyl]-N-[2-(4-sulfamoylphenyl)ethyl]glycinamide
InChI=1S/C15H19N3O4S/c16-10-15(19)18(11-13-2-1-9-22-13)8-7-12-3-5-14(6-4-12)23(17,20)21/h1-6,9H,7-8,10-11,16H2,(H2,17,20,21)
c1cc(oc1)CN(CCc2ccc(cc2)S(=O)(=O)N)C(=O)CN
Y
1,144
7GSZ
X-RAY DIFFRACTION
3.39
63.77
VAPOR DIFFUSION, SITTING DROP
7.5
0.3 M magnesium acetate, 0.1 M HEPES pH 7.5, 0.1% beta-mercaptoethanol, 13-14% PEG 8000, 2% ethanol
277
2024-01-03
2024-01-24
2,556
1
321
245
null
37.67
1
1.91
experimental
44.292
0.2409
0.1996
PanDDA Analysis group deposition -- Crystal structure of PTP1B in complex with FMSOA000686b
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPSRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTVGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHN
Protein
321
polypeptide(L)
1
37.346
Tyrosine-protein phosphatase non-receptor type 1
3.1.3.48
PDB Primary Data
Homo sapiens
9,606
321
1
1
1
Monomer
A1
TRS
C4 H12 N O3
122.143
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
InChI=1S/C4H11NO3/c5-4(1-6,2-7)3-8/h6-8H,1-3,5H2/p+1
C(C(CO)(CO)[NH3+])O
null
9,757
5B6C
X-RAY DIFFRACTION
2.33
47.18
VAPOR DIFFUSION, HANGING DROP
7.5
21%(w/v) PEG 8000, 2.9mM n-nonyl-beta-thiomaltoside, 0.1M HEPES, pH 7.5
293.15
2016-05-26
2017-01-04
1,740
2
185
274
null
20.94
2
1.55
experimental
17.623
0.1995
0.15797
Structural Details of Ufd1 binding to p97
GSNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKRA
Protein
174
polypeptide(L)
1
19.726
Transitional endoplasmic reticulum ATPase
3.6.4.6
PDB Primary Data
Homo sapiens
9,606
185
2
2
1
Hetero 2-mer
A1, B1
null
null
null
null
null
null
null
9,671
7MHD
X-RAY DIFFRACTION
1.97
37.64
VAPOR DIFFUSION, SITTING DROP
null
0.3 ul of 8 mg/ml FASN-TE in 100 mM NaCl, 50 mM BisTris pH 6.0, 10 mM DTT, 0.5 mM of the inhibitor and 1% DMSO were mixed with 0.2 ul of well solution 10% PEG400, 50 mM TRIS-Cl pH 8.5, 1 mM DTT, 1 mM Ethylenediaminetetraacetic acid disodium salt (EDTA), 300 mM NaCl.
293
2021-04-15
2022-04-20
2,374
1
298
106
null
32.93
1
2.03
experimental
42.494
0.2457
0.1928
Thioesterase Domain of Human Fatty Acid Synthase (FASN-TE) binding a competitive inhibitor SBP-7635
GSGGGGGSTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEH
Protein
298
polypeptide(L)
1
32.525
Fatty acid synthase
3.1.2.14
PDB Primary Data
Homo sapiens
9,606
298
1
1
1
Monomer
A1
ZEP
C20 H21 F N2 O2 S2
404.521
N,N-diethyl-4-{2-[(2-fluorophenyl)methyl]-1,3-thiazol-4-yl}benzene-1-sulfonamide
InChI=1S/C20H21FN2O2S2/c1-3-23(4-2)27(24,25)17-11-9-15(10-12-17)19-14-26-20(22-19)13-16-7-5-6-8-18(16)21/h5-12,14H,3-4,13H2,1-2H3
CCN(CC)S(=O)(=O)c1ccc(cc1)c2csc(n2)Cc3ccccc3F
Y
2,510
5HYN
X-RAY DIFFRACTION
2.82
56.33
VAPOR DIFFUSION, SITTING DROP
6.5
25% PEG3350, 400mM Ammonian Citrate pH6.5
291
2016-02-01
2016-05-11
35,028
20
5,068
null
null
586.82
5
2.95
experimental
null
0.2733
0.2191
Structure of Human Polycomb Repressive Complex 2 (PRC2) with oncogenic histone H3K27M peptide
ATKAARMSAPATG
Protein
13
polypeptide(L)
4
1.234
H3K27M
null
null
Homo sapiens
9,606
1,267
5
5
1
Hetero 5-mer
A1, B1, C1, D1, E1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
10,332
8SWC
X-RAY DIFFRACTION
2.6
52.61
VAPOR DIFFUSION, HANGING DROP
null
2:1 complex : precipitant (0.1 M sodium acetate, pH 4.6, 8% w/v PEG4000), cryoprotection: mother liquor + 25% v/v glycerol, 1 minute
277
2023-05-18
2024-06-19
2,052
3
334
5
null
46.62
1
2.68
experimental
83.64
0.22
0.1915
RNase H complex with ASO (OOO) and RNA
HHHHHHHHMSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTNSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
Protein
294
polypeptide(L)
1
33.218
Ribonuclease H1
3.1.26.4
PDB Primary Data
Homo sapiens
9,606
334
3
3
1
Monomer
A1
PO4
O4 P
94.971
PHOSPHATE ION
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
[O-]P(=O)([O-])[O-]
null
2,273
6EKN
X-RAY DIFFRACTION
2.16
43.15
VAPOR DIFFUSION, SITTING DROP
10
Protein: 1 micro-L MMP12 at 290 micro-M with 10 milli-M acetohydroxamate + 0.1 Micro-L BE6 from 10 milii-M in 100% DMSO Precipitant: 17% PEG 20K, 250 milli-M NaCl, 100 milii-M TRIS HCl, pH 10.0. cryoprotectant: 40% (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol) 10 % PEG 10K, 200 milli-M NaCl, 100 milli-M AAB (Na acetate,N-(2-Acetamido)iminodiacetic acid (ADA), Bicine) 10% acid/90% basic
293
2017-09-26
2018-05-16
1,548
1
159
151
null
18.38
1
1.2
experimental
20.711
0.17523
0.1442
Crystal structure of MMP12 in complex with inhibitor BE7.
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
Protein
159
polypeptide(L)
1
17.616
Macrophage metalloelastase
3.4.24.65
PDB Primary Data
Homo sapiens
9,606
159
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
5,767
5V05
X-RAY DIFFRACTION
2.65
53.52
VAPOR DIFFUSION, SITTING DROP
7
100 mM sodium acetate, pH 7.0, 10 mM potassium chloride, 2-4% PEG4000
290
2017-02-28
2017-05-24
3,253
3
381
54
null
47.48
1
2.902
experimental
null
0.2484
0.1992
Crystal structure of human exonuclease 1 Exo1 (WT) in complex with 5' recessed-end DNA (rIII)
MGIQGLLQFIKEASEPIHVRKYKGQVVAVDTYCWLHKGAIACAEKLAKGEPTDRYVGFCMKFVNMLLSHGIKPILVFDGCTLPSKKEVERSRRERRQANLLKGKQLLREGKVSEARECFTRSINITHAMAHKVIKAARSQGVDCLVAPYEADAQLAYLNKAGIVQAIITEDSDLLAFGCKKVILKMDQFGNGLEIDQARLGMCRQLGDVFTEEKFRYMCILSGCDYLSSLRGIGLAKACKVLRLANNPDIVKVIKKIGHYLKMNITVPEDYINGFIRANNTFLYQLVFDPIKRKLIPLNAYEDDVDPETLSYAGQYVDDSIALQIALGNKDINTFEQIDDYNPDTAMPAHSRENLYFQ
Protein
358
polypeptide(L)
1
40.355
Exonuclease 1
3.1
PDB Primary Data
Homo sapiens
9,606
381
3
3
1
Monomer
A1
MN
Mn
54.938
MANGANESE (II) ION
InChI=1S/Mn/q+2
[Mn+2]
null
5,226
5F6V
X-RAY DIFFRACTION
2.71
54.63
VAPOR DIFFUSION, HANGING DROP
8.5
0.1M Tris pH 8.5, 8% (w/v) polyethylene glycol 8000
294
2015-12-07
2016-04-27
1,582
1
157
228
null
17.91
1
1.492
experimental
null
0.1838
0.1519
Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol from fragment cocktail screen)
SGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGAAGTPWAGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
Protein
157
polypeptide(L)
1
17.725
SUMO-conjugating enzyme UBC9
6.3.2
PDB Primary Data
Homo sapiens
9,606
157
1
1
1
Monomer
A1
5VL
C12 H10 O2
186.207
2-(2-hydroxyphenyl)phenol
InChI=1S/C12H10O2/c13-11-7-3-1-5-9(11)10-6-2-4-8-12(10)14/h1-8,13-14H
c1ccc(c(c1)c2ccccc2O)O
null
5,938
6QFE
X-RAY DIFFRACTION
2.97
58.59
VAPOR DIFFUSION, SITTING DROP
5.6
100mM Sodium Citrate pH 5.6, 20% PEG 4K, 5% Glycerol, 10% Iso-propanol
293
2019-01-10
2019-05-08
4,083
2
454
393
12
52.52
1
1.67
experimental
30.43
0.242
0.211
Crystal Structure of Human Kallikrein 5 in complex with GSK144
IINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS
Protein
227
polypeptide(L)
2
25.193
Kallikrein-5
3.4.21
PDB Primary Data
Homo sapiens
9,606
227
1
1
1
Monomer
A1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
10,458
6DKB
X-RAY DIFFRACTION
2.29
46.23
VAPOR DIFFUSION, SITTING DROP
8
Well volume: 30.0 uL Drop volume from well: 0.2 uL Drop protein volume: 0.4 uL Well Ingredients: Polymer: 10.0 %w/v (6.0 uL of stock 50.0 %w/v) PEG 3350 Buffer: 16.0 %v/v (4.8 uL of stock 100.0 %v/v) tacsimate (pH 8.00) Organic (non-volatile): 10.0 %v/v (3.0 uL of stock 100.0 %v/v) Ethylene glycol Additive: 0.025 M (1.5 uL of stock 0.5 M) TCEP hydrochloride Plate setup temperature: 13 C Plate incubation temperature: 21 C
294
2018-05-29
2018-07-11
2,222
1
320
1
null
36.63
1
2.68
experimental
80.37
0.245
0.2159
Crystal structure of Trk-A in complex with the Pan-Trk Kinase Inhibitor, compound 10b.
GSTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG
Protein
320
polypeptide(L)
1
36.111
High affinity nerve growth factor receptor
2.7.10.1
PDB Primary Data
Homo sapiens
9,606
320
1
1
1
Monomer
A1
FKY
C24 H23 F4 N5 O4
521.464
2-{[(3R,4S)-3-fluoro-1-{[4-(trifluoromethoxy)phenyl]acetyl}piperidin-4-yl]oxy}-5-(1-methyl-1H-imidazol-4-yl)pyridine-3-carboxamide
InChI=1S/C24H23F4N5O4/c1-32-12-19(31-13-32)15-9-17(22(29)35)23(30-10-15)36-20-6-7-33(11-18(20)25)21(34)8-14-2-4-16(5-3-14)37-24(26,27)28/h2-5,9-10,12-13,18,20H,6-8,11H2,1H3,(H2,29,35)/t18-,20+/m1/s1
Cn1cc(nc1)c2cc(c(nc2)OC3CCN(CC3F)C(=O)Cc4ccc(cc4)OC(F)(F)F)C(=O)N
null
6,112
6N2S
X-RAY DIFFRACTION
2.23
44.74
VAPOR DIFFUSION, SITTING DROP
null
16-18% PEG 2000 Monomethyl Ether
291
2018-11-14
2019-03-27
3,356
4
366
81
null
48.31
1
2.457
experimental
44.6413
0.2896
0.2024
Ternary complex crystal structure of DNA polymerase Beta with 5-carboxy-dC (5-caC) at the templating position
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
Protein
335
polypeptide(L)
1
38.242
DNA polymerase beta
2.7.7.7
PDB Primary Data
Homo sapiens
9,606
366
4
4
1
Monomer
A1
MG
Mg
24.305
MAGNESIUM ION
InChI=1S/Mg/q+2
[Mg+2]
null
102
8J7Q
X-RAY DIFFRACTION
2.76
55.44
VAPOR DIFFUSION
null
0.2 M (NH4)2SO4, 20% PEG8000, 100 mM MES PH6.0
289
2023-04-28
2024-04-03
2,249
1
289
196
null
32.55
1
1.69
experimental
null
0.2456
0.2155
The active site mutant of human inorganic pyrophosphatase
MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKGKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGANAAIAVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN
Protein
289
polypeptide(L)
1
32.547
Inorganic pyrophosphatase
3.6.1.1
PDB Primary Data
Homo sapiens
9,606
289
1
1
1
Monomer
A1
null
null
null
null
null
null
null
1,989
4WLR
X-RAY DIFFRACTION
2.63
53.27
VAPOR DIFFUSION, SITTING DROP
6.6
25% PEG 3350, 220 mM MgCl2,100 mM Bis-Tris
277
2014-10-07
2015-03-04
3,920
3
506
201
null
56.83
3
1.997
experimental
null
0.2273
0.1806
Crystal Structure of mUCH37-hRPN13 CTD-hUb complex
MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPESFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTPAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
Protein
328
polypeptide(L)
1
37.534
Ubiquitin carboxyl-terminal hydrolase isozyme L5
3.4.19.12
PDB Primary Data
Mus musculus
10,090
506
3
3
1
Hetero 3-mer
A1, B1, C1
null
null
null
null
null
null
null
6,832
7MNI
X-RAY DIFFRACTION
2.08
40.93
VAPOR DIFFUSION, HANGING DROP
8.3
20% w/v PEG4000, 0.22 M sodium chloride, 0.1 M Tris
294
2021-05-01
2022-06-15
9,442
4
1,294
418
null
143.79
2
2
experimental
61.7063
0.2084
0.1752
Crystal structure of the N-terminal domain of NUP88 in complex with NUP98 C-terminal Autoproteolytic Domain
SMAAAEGPVGDGELWQTWLPNHVVFLRLREGLKNQSPTEAEKPASSSLPSSPPPQLLTRNVVFGLGGELFLWDGEDSSFLVVRLRGPSGGGEEPALSQYQRLLCINPPLFEIYQVLLSPTQHHVALIGIKGLMVLELPKRWGKNSEFEGGKSTVNCSTTPVAERFFTSSTSLTLKHAAWYPSEILDPHVVLLTSDNVIRIYSLREPQTPTNVIILSEAEEESLVLNKGRAYTASLGETAVAFDFGPLAAVPKTLFGQNGKDEVVAYPLYILYENGETFLTYISLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAVLCLPCVPNILVIATESGMLYHCVVLEGEEEDDHTSEKSWDSRIDLIPSLYVFECVELELALKLASGEDDPFDSDFSCPVKLHRDPKCPSRYHCTHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELSTEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPTMICITSTYECLIWP
Protein
494
polypeptide(L)
2
54.635
Nuclear pore complex protein Nup88
null
null
Homo sapiens
9,606
647
2
2
1
Hetero 2-mer
A1, B1
null
null
null
null
null
null
null
4,639
6Q49
X-RAY DIFFRACTION
1.99
38.2
VAPOR DIFFUSION, HANGING DROP
7.4
10MG/ML CDK2 10% V/V PEG3350, 50 MM HEPES/NAOH, 50 MM NA/K PHOSPHATE, PH 7.5
293
2018-12-05
2019-03-20
2,771
1
306
305
null
35.01
1
1.0
experimental
23.835
0.19718
0.17524
CDK2 in complex with FragLite6
GPLGSPEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
Protein
306
polypeptide(L)
1
34.761
Cyclin-dependent kinase 2
2.7.11.22
PDB Primary Data
Homo sapiens
9,606
306
1
1
1
Monomer
A1
DMS
C2 H6 O S
78.133
DIMETHYL SULFOXIDE
InChI=1S/C2H6OS/c1-4(2)3/h1-2H3
CS(=O)C
null
7,882
5L0S
X-RAY DIFFRACTION
2.41
49.04
VAPOR DIFFUSION, HANGING DROP
6.5
20% PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% glycerol
295
2016-07-28
2017-08-09
3,747
2
399
377
7
47.89
2
1.45
experimental
29.8733
0.1588
0.1394
human POGLUT1 in complex with Factor VII EGF1 and UDP
GSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTHYQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLVDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWLEFFYPQLKPWVHYIPVKTDLSNVQELLQFVKANDDVAQEIAERGSQFIRNHLQMDDITCYWENLLSEYSKFLSYNVTRRKGYDQIIP
Protein
357
polypeptide(L)
1
42.077
Protein O-glucosyltransferase 1
2.4.1
PDB Primary Data
Homo sapiens
9,606
399
2
2
1
Hetero 2-mer
A1, B1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
828
7JWE
X-RAY DIFFRACTION
2.32
46.95
VAPOR DIFFUSION, SITTING DROP
7.5
100 mM Tris pH 7.5, 250 mM (NH4)2SO4 and 20-22% PEG 4000
298
2020-08-25
2021-03-17
6,666
1
966
9
null
111.34
1
2.55
experimental
88.8962
0.2529
0.209
Gedatolisib bound to the PI3Kg catalytic subunit p110 gamma
MSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSAHHHHHH
Protein
966
polypeptide(L)
1
110.727
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
2.7.1.153
PDB Primary Data
Homo sapiens
9,606
966
1
1
1
Monomer
A1
VL1
C32 H41 N9 O4
615.726
Gedatolisib
InChI=1S/C32H41N9O4/c1-38(2)27-11-13-39(14-12-27)29(42)24-5-9-26(10-6-24)34-32(43)33-25-7-3-23(4-8-25)28-35-30(40-15-19-44-20-16-40)37-31(36-28)41-17-21-45-22-18-41/h3-10,27H,11-22H2,1-2H3,(H2,33,34,43)
CN(C)C1CCN(CC1)C(=O)c2ccc(cc2)NC(=O)Nc3ccc(cc3)c4nc(nc(n4)N5CCOCC5)N6CCOCC6
Y
8,627
4YPE
X-RAY DIFFRACTION
2.31
46.69
VAPOR DIFFUSION, SITTING DROP
null
PEG 3350, 20 mM Tris
277
2015-03-12
2015-09-02
3,572
2
452
107
2
53.24
1
2.2
experimental
32.169
0.2625
0.2165
ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM)
GAMAGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDFYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGGKSQRVNG
Protein
226
polypeptide(L)
2
26.026
Histone-lysine N-methyltransferase ASH1L
2.1.1.43
PDB Primary Data
Homo sapiens
9,606
226
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
1,672
6Q8K
X-RAY DIFFRACTION
2.4
48.76
VAPOR DIFFUSION, SITTING DROP
9
255 PEG 6000. 0.1 M bicine pH 9.0
277
2018-12-14
2019-02-20
2,916
1
339
129
null
39.98
1
2.29
experimental
35.14
0.25916
0.18779
CLK1 with bound pyridoquinazoline
SMHLICQSGDVLSARYEIVDTLGEGAFGKVVECIDHKAGGRHVAVKIVKNVDRYCEAARSEIQVLEHLNTTDPNSTFRCVQMLEWFEHHGHICIVFELLGLSTYDFIKENGFLPFRLDHIRKMAYQICKSVNFLHSNKLTHTDLKPENILFVQSDYTEAYNPKIKRDERTLINPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFPTHDSKEHLAMMERILGPLPKHMIQKTRKRKYFHHDRLDWDEHSSAGRYVSRACKPLKEFMLSQDVEHERLFDLIQKMLEYDPAKRITLREALKHPFFDLLKKSI
Protein
339
polypeptide(L)
1
39.582
Dual specificity protein kinase CLK1
2.7.12.1
PDB Primary Data
Homo sapiens
9,606
339
1
1
1
Monomer
A1
EDO
C2 H6 O2
62.068
1,2-ETHANEDIOL
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
C(CO)O
null
5,770
7UY0
X-RAY DIFFRACTION
2.96
58.4
VAPOR DIFFUSION
7.5
For co-crystallization with A-419259, Fgr (3.2 mg/mL in 20 mM Tris-HCl, pH 8.3, 100 mM NaCl, and 2 mM TCEP) was mixed with 10 mM A-419259 (in 50% DMSO) to a final inhibitor concentration of 120 microM (0.3% DMSO final) and incubated for 30 min at 298 K prior to crystallization setup. Crystals were grown by sitting- and hanging-drop vapor diffusion at 277 K by mixing Fgr/A-419259 in a 1:1 ratio with the mother liquor (0.2 M sodium/potassium phosphate, 0.1 M Bis-Tris propane, pH 7.5, and 16% PEG 3350). To promote crystal growth, crystal seeds from initial needle-like crystals were added to the crystallization drops
277
2022-05-06
2022-12-28
7,349
2
912
50
null
106.13
2
2.55
experimental
71.1545
0.2229
0.1865
Crystal structure of human Fgr tyrosine kinase in complex with A-419259
MGHHHHHHTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQLYAVVSEEPIYIVTEFMCHGSLLDFLKNPEGQDLRLPQLVDMAAQVAEGMAYMERMNYIHRDLRAANILVGERLACKIADFGLARLIKDDEYNPCQGSKFPIKWTAPEAALFGRFTIKSDVWSFGILLTELITKGRIPYPGMNKREVLEQVEQGYHMPCPPGCPASLYEAMEQTWRLDPEERPTFEYLQSFLEDYFTSAEPQYEEIP
Protein
456
polypeptide(L)
1
52.241
Tyrosine-protein kinase Fgr
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
456
1
1
1
Monomer
A1
GOL
C3 H8 O3
92.094
GLYCEROL
InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
C(C(CO)O)O
null
8,621
6J5L
X-RAY DIFFRACTION
3.11
60.42
VAPOR DIFFUSION, SITTING DROP
5.3
0.65 M Ammonium sulfate, 0.1 M Sodium Citrate pH 5.3
293
2019-01-11
2019-07-17
2,220
1
303
32
null
34.74
1
2.3
experimental
69.112
0.25078
0.22312
Crystal structure of Trk-A in complex with the Pan-Trk Kinase Inhibitor, compound 10e
GAMGSGIRVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG
Protein
303
polypeptide(L)
1
34.262
High affinity nerve growth factor receptor
2.7.10.1
PDB Primary Data
Homo sapiens
9,606
303
1
1
1
Monomer
A1
B9C
C24 H27 N7 O2 S
477.582
N-{2-[({3-[6-(piperazin-1-yl)pyridin-3-yl]-1H-indazol-5-yl}amino)methyl]phenyl}methanesulfonamide
InChI=1S/C24H27N7O2S/c1-34(32,33)30-21-5-3-2-4-17(21)15-26-19-7-8-22-20(14-19)24(29-28-22)18-6-9-23(27-16-18)31-12-10-25-11-13-31/h2-9,14,16,25-26,30H,10-13,15H2,1H3,(H,28,29)
CS(=O)(=O)Nc1ccccc1CNc2ccc3c(c2)c(n[nH]3)c4ccc(nc4)N5CCNCC5
Y
9,156
4UFY
X-RAY DIFFRACTION
2.5
50
null
8.5
0.2 M LISO4, 0.1 M TRIS HCL, 22% PEG3350, PH 8.5
null
2015-03-20
2016-04-13
3,947
2
480
460
null
55.89
1
1.7
experimental
24.074
0.19125
0.16727
Crystal structure of human tankyrase 2 in complex with TA-13
MHHHHHHSSGVDLGTENLYFQSMLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIMRPEG
Protein
240
polypeptide(L)
2
27.3
TANKYRASE-2
2.4.2.30
PDB Primary Data
Homo sapiens
9,606
240
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
5,972
4Q0L
X-RAY DIFFRACTION
1.92
35.4
VAPOR DIFFUSION, SITTING DROP
5
Crystallization buffer: 0.1M ammonium citrate with pH 5.0 and 18% of PEG4000, VAPOR DIFFUSION, SITTING DROP, temperature 291K
291
2014-04-02
2015-01-28
8,894
4
1,052
320
4
121.71
1
2
experimental
20.194
0.328
0.264
Crystal structure of catalytic domain of human carbonic anhydrase isozyme XII with inhibitor
MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGLQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSHLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPREMINNFRQVQKFDERLVYTSFSQ
Protein
263
polypeptide(L)
4
29.917
Carbonic anhydrase 12
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
526
2
2
1
Homo 2-mer
A2
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
2,856
5JNT
X-RAY DIFFRACTION
2.47
50.11
EVAPORATION
6.5
20% PEG 3350, 200 mM NaCl, 40 mM MES
293
2016-04-30
2017-03-29
1,591
1
160
275
null
18.64
1
1.45
experimental
15.964
0.1658
0.1346
Crystal structure of human low molecular weight protein tyrosine phosphatase (LMPTP) type A complexed with MES
GSMAEQVTKSVLFVCLGNICRSPIAEAVFRKLVTDQNISENWRVDSAATSGYEIGNPPDYRGQSCMKRHGIPMSHVARQITKEDFATFDYILCMDESNLRDLNRKSNQVKTCKAKIELLGSYDPQKQLIIEDPYYGNDSDFETVYQQCVRCCRAFLEKAH
Protein
160
polypeptide(L)
1
18.238
Low molecular weight phosphotyrosine protein phosphatase
3.1.3.48
PDB Primary Data
Homo sapiens
9,606
160
1
1
1
Monomer
A1
MES
C6 H13 N O4 S
195.237
2-(N-MORPHOLINO)-ETHANESULFONIC ACID
InChI=1S/C6H13NO4S/c8-12(9,10)6-3-7-1-4-11-5-2-7/h1-6H2,(H,8,9,10)
C1COCC[NH+]1CCS(=O)(=O)[O-]
null
6,700
4RSS
X-RAY DIFFRACTION
2.12
42.11
VAPOR DIFFUSION, HANGING DROP
8.5
10-20% (v/v) PEG 3350, 100mM Tris-HCl (pH 8.5) , VAPOR DIFFUSION, HANGING DROP, temperature 277K
277
2014-11-11
2015-10-21
2,414
1
290
178
null
34.32
1
1.83
experimental
32.173
0.24869
0.21189
Crystal structure of tyrosine-protein kinase SYK with an inhibitor
EEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVELRLRNYYYDVVNLEHHHHHHHH
Protein
290
polypeptide(L)
1
33.901
Tyrosine-protein kinase SYK
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
290
1
1
1
Monomer
A1
4MG
C23 H27 N7 O
417.507
1-[(3-methyl-1-{2-[(1,2,3-trimethyl-1H-indol-5-yl)amino]pyrimidin-4-yl}-1H-pyrazol-4-yl)methyl]azetidin-3-ol
InChI=1S/C23H27N7O/c1-14-16(3)28(4)21-6-5-18(9-20(14)21)25-23-24-8-7-22(26-23)30-11-17(15(2)27-30)10-29-12-19(31)13-29/h5-9,11,19,31H,10,12-13H2,1-4H3,(H,24,25,26)
Cc1c(n(c2c1cc(cc2)Nc3nccc(n3)n4cc(c(n4)C)CN5CC(C5)O)C)C
null
11,516
4XG9
X-RAY DIFFRACTION
2.12
41.85
VAPOR DIFFUSION, HANGING DROP
8.5
10~20%(v/v) PEG3350, 100 mM Tris-HCl
278
2014-12-30
2015-12-30
4,325
2
580
3
null
68.68
1
2.91
experimental
49.781
0.24104
0.2085
Crystal structure of an inhibitor-bound Syk
EEIRPKEVYLDRKLLTLEDKELGSGNFGTVKKGYYQMKKVVKTVAVKILKNEANDPALKDELLAEANVMQQLDNPYIVRMIGICEAESWMLVMEMAELGPLNKYLQQNRHVKDKNIIELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGKWPVKWYAPECINYYKFSSKSDVWSFGVLMWEAFSYGQKPYRGMKGSEVTAMLEKGERMGCPAGCPREMYDLMNLCWTYDVENRPGFAAVELRLRNYYYDVVNLEHHHHHHHH
Protein
290
polypeptide(L)
2
33.901
Tyrosine-protein kinase SYK
2.7.10.2
PDB Primary Data
Homo sapiens
9,606
290
1
1
1
Monomer
A1
X9G
C22 H24 Cl N7 O
437.925
1-[(1-{2-[(3-chloro-1,2-dimethyl-1H-indol-5-yl)amino]pyrimidin-4-yl}-3-methyl-1H-pyrazol-4-yl)methyl]azetidin-3-ol
InChI=1S/C22H24ClN7O/c1-13-15(9-29-11-17(31)12-29)10-30(27-13)20-6-7-24-22(26-20)25-16-4-5-19-18(8-16)21(23)14(2)28(19)3/h4-8,10,17,31H,9,11-12H2,1-3H3,(H,24,25,26)
Cc1c(cn(n1)c2ccnc(n2)Nc3ccc4c(c3)c(c(n4C)C)Cl)CN5CC(C5)O
null
11,618
6GLH
X-RAY DIFFRACTION
1.72
28.54
VAPOR DIFFUSION, HANGING DROP
4.5
crystallized in: 23-27% PEG3350, 0.2 M LiSO4, 0.1 M sodium acetate pH 4.5 soaked in: 0.27 M ammonium sulfate, 17% glycerol, 27% PEG4000, 20% DMSO, 10 mM compound
293
2018-05-23
2019-02-20
1,517
1
182
212
null
21.36
1
1.201
experimental
null
0.2014
0.1935
Crystal structure of hMTH1 F27A in complex with LW14 in the absence of acetate
MKHHHHHHPMSDYDIPTTENLYFQGAMGASRLYTLVLVLQPQRVLLGMKKRGAGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV
Protein
182
polypeptide(L)
1
21.029
7,8-dihydro-8-oxoguanine triphosphatase
3.6.1.55
PDB Primary Data
Homo sapiens
9,606
182
1
1
1
Monomer
A1
BU8
C6 H6 N4
134.139
1~{H}-imidazo[4,5-b]pyridin-2-amine
InChI=1S/C6H6N4/c7-6-9-4-2-1-3-8-5(4)10-6/h1-3H,(H3,7,8,9,10)
c1cc2c(nc1)nc([nH]2)N
null
2,275
5EW1
X-RAY DIFFRACTION
2.73
55.02
VAPOR DIFFUSION, HANGING DROP
6.5
28% MPEG 2000, 0.1 M Bis/Tris pH 6.5
298
2015-11-20
2016-11-30
3,214
4
337
74
4
47.7
2
2.95
experimental
50.954
0.208
0.1555
Human thrombin sandwiched between two DNA aptamers: HD22 and HD1-deltaT3
TFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR
Protein
36
polypeptide(L)
1
4.097
thrombin light chain
3.4.21.5
PDB Primary Data
Homo sapiens
9,606
337
4
4
1
Hetero 2-mer
A1, B1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
11,656
5PAJ
X-RAY DIFFRACTION
null
null
VAPOR DIFFUSION, SITTING DROP
8.5
16 mg/ml protein in 20mM Tris/HCl pH 8.4, 5 mM benzamidine, 0.1 M NaCl, 50 mM CaCl2 mixed 1+1 with 32-35% AMMONIUM SULPHATE, 2% PEG 4000, 0.1 M Bicine-NaOH pH 8.5, 15% glycerol
277
2016-11-10
2017-06-21
2,808
2
318
280
8
35.88
2
1.7
experimental
24.376
0.2241
0.2
Crystal Structure of Factor VIIa in complex with 1-(1-aminoisoquinolin-6-yl)-3-benzylurea
LICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGR
Protein
64
polypeptide(L)
1
6.985
Coagulation factor VII light chain
3.4.21.21
PDB Primary Data
Homo sapiens
9,606
318
2
2
1
Hetero 2-mer
A1, B1
7XJ
C17 H16 N4 O
292.335
1-(1-azanylisoquinolin-6-yl)-3-(phenylmethyl)urea
InChI=1S/C17H16N4O/c18-16-15-7-6-14(10-13(15)8-9-19-16)21-17(22)20-11-12-4-2-1-3-5-12/h1-10H,11H2,(H2,18,19)(H2,20,21,22)
c1ccc(cc1)CNC(=O)Nc2ccc3c(c2)ccnc3N
null
7,413
5LUA
X-RAY DIFFRACTION
2.34
47.41
VAPOR DIFFUSION, SITTING DROP
null
22 % PEG 3350, 0.1 M sodium acetate pH 4.5
293
2016-09-08
2017-03-29
4,609
2
524
272
null
61.87
1
2
experimental
27.4
0.252
0.222
Crystal structure of human legumain (AEP) in complex with compound 11b
GGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIVVMMYDDIAYSEDNPTPGIVINRPNGTDVYQGVPKDYTGEDVTPQNFLAVLRGDAEAVKGIGSGKVLKSGPQDHVFIYFTNHGSTGILVFPNEDLHVKDLNETIHYMYKHKMYRKMVFYIEACESGSMMNHLPDNINVYATTAANPRESSYACYYDEKRSTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTQTSHVMQYGNKTISTMKVMQFQGMK
Protein
262
polypeptide(L)
2
29.945
Legumain
3.4.22.34
PDB Primary Data
Homo sapiens
9,606
262
1
1
1
Monomer
A1
NAG
C8 H15 N O6
221.208
2-acetamido-2-deoxy-beta-D-glucopyranose
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
CC(=O)NC1C(C(C(OC1O)CO)O)O
null
6,908
6YOL
X-RAY DIFFRACTION
2.11
41.58
VAPOR DIFFUSION, HANGING DROP
7.8
1.6 M sodium citrate, 50 mM Tris-H2SO4
291
2020-04-14
2020-08-19
2,389
1
260
282
null
29.51
1
1.15
experimental
18.945
0.1705
0.1409
Meta-Nidocarborane propyl-sulfonamide in complex with CA IX mimic
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVTFDDSQDKAVLKGGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTEGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
Protein
260
polypeptide(L)
1
29.201
Carbonic anhydrase 2
4.2.1.1
PDB Primary Data
Homo sapiens
9,606
260
1
1
1
Monomer
A1
ZN
Zn
65.409
ZINC ION
InChI=1S/Zn/q+2
[Zn+2]
null
2,045
7OVJ
X-RAY DIFFRACTION
2.42
49.08
VAPOR DIFFUSION, HANGING DROP
null
180-220 mM sodium citrate, 15-25 % PEG3350
277
2021-06-15
2022-07-20
2,237
1
318
77
null
36.66
1
2.35
experimental
57.81
0.2445
0.2017
Protein kinase MKK7 in complex with difluoro-phenethyltriazole-substituted pyrazolopyrimidine
MGHHHHHHSAKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTRSPRTSG
Protein
318
polypeptide(L)
1
36.175
Dual specificity mitogen-activated protein kinase kinase 7
2.7.12.2
PDB Primary Data
Homo sapiens
9,606
318
1
1
1
Monomer
A1
24N
C23 H25 F2 N9 O
481.501
1-[(3~{R})-3-[4-azanyl-3-[1-[2,2-bis(fluoranyl)-2-phenyl-ethyl]-1,2,3-triazol-4-yl]pyrazolo[3,4-d]pyrimidin-1-yl]piperidin-1-yl]propan-1-one
InChI=1S/C23H25F2N9O/c1-2-18(35)32-10-6-9-16(11-32)34-22-19(21(26)27-14-28-22)20(30-34)17-12-33(31-29-17)13-23(24,25)15-7-4-3-5-8-15/h3-5,7-8,12,14,16H,2,6,9-11,13H2,1H3,(H2,26,27,28)/t16-/m1/s1
CCC(=O)N1CCCC(C1)n2c3c(c(n2)c4cn(nn4)CC(c5ccccc5)(F)F)c(ncn3)N
Y
6,571
6BG0
X-RAY DIFFRACTION
2.26
45.53
VAPOR DIFFUSION, HANGING DROP
null
Crystals were obtained at 18 C by the hanging drop vapor diffusion method using 4 mL drops that contained equal volumes of protein and reservoir solutions over a 0.5 mL solution of 100 mM sodium citrate, pH 4.9-5.2, 8-18 % PEG 6000 (w/v), 10 mM DTT, and 3 mM NaN3. Crystals appeared within 3-5 days and were briefly immersed in a cryogenic solution containing 10% MPD (2-methylpentane-2,4-diol) and 90% reservoir solution.
291
2017-10-27
2018-02-21
4,244
6
566
346
null
64.46
3
2.125
experimental
null
0.2011
0.1606
Caspase-3 Mutant - D9A,D28A,S150D
MENTENSVASKSIKNLEPKIIHGSESMASGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRDLTGKPKLFIIQACRGTELDCGIETD
Protein
175
polypeptide(L)
2
19.699
Caspase-3
3.4.22.56
PDB Primary Data
Homo sapiens
9,606
283
3
3
1
Hetero 3-mer
A1, B1, C1
null
Na
22.99
SODIUM ION
InChI=1S/Na/q+1
[Na+]
null
9,909