Structure of PDB 3ruk Chain C Binding Site BS02

Receptor Information
>3ruk Chain C (length=472) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQ
LAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMA
TFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLE
KLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGP
DQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYE
EIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSS
IGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSV
SYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIP
KVVFLIDSFKVKIKVRQAWREA
Ligand information
Ligand IDAER
InChIInChI=1S/C24H31NO/c1-23-11-9-18(26)14-17(23)5-6-19-21-8-7-20(16-4-3-13-25-15-16)24(21,2)12-10-22(19)23/h3-5,7,13,15,18-19,21-22,26H,6,8-12,14H2,1-2H3/t18-,19-,21-,22-,23-,24+/m0/s1
InChIKeyGZOSMCIZMLWJML-VJLLXTKPSA-N
SMILES
SoftwareSMILES
CACTVS 3.370C[C]12CC[CH](O)CC1=CC[CH]3[CH]2CC[C]4(C)[CH]3CC=C4c5cccnc5
CACTVS 3.370C[C@]12CC[C@H](O)CC1=CC[C@@H]3[C@@H]2CC[C@@]4(C)[C@H]3CC=C4c5cccnc5
OpenEye OEToolkits 1.7.2C[C@]12CC[C@@H](CC1=CC[C@@H]3[C@@H]2CC[C@]4([C@H]3CC=C4c5cccnc5)C)O
ACDLabs 12.01OC4CC3=CCC5C2C(C(c1cccnc1)=CC2)(C)CCC5C3(C)CC4
OpenEye OEToolkits 1.7.2CC12CCC(CC1=CCC3C2CCC4(C3CC=C4c5cccnc5)C)O
FormulaC24 H31 N O
NameAbiraterone;
(3S,8R,9S,10R,13S,14S)-10,13-dimethyl-17-pyridin-3-yl-2,3,4,7,8,9,11,12,14,15-decahydro-1H-cyclopenta[a]phenanthren-3-ol
ChEMBLCHEMBL254328
DrugBankDB05812
ZINCZINC000003797541
PDB chain3ruk Chain C Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ruk Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		A113 Y201 N202 T306
Binding residue
(residue number reindexed from 1)		A83 Y171 N172 T276
Annotation score2
Binding affinityBindingDB: IC50=72nM
Enzymatic activity
Catalytic site (original residue number in PDB) T306 F435 C442
Catalytic site (residue number reindexed from 1) T276 F405 C412
Enzyme Commision number 1.14.14.19: steroid 17alpha-monooxygenase.
1.14.14.32: 17alpha-hydroxyprogesterone deacetylase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004508 steroid 17-alpha-monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016829 lyase activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006694 steroid biosynthetic process
GO:0006702 androgen biosynthetic process
GO:0006704 glucocorticoid biosynthetic process
GO:0007548 sex differentiation
GO:0008202 steroid metabolic process
GO:0042445 hormone metabolic process
GO:0042446 hormone biosynthetic process
GO:0042448 progesterone metabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0030424 axon
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ruk, PDBe:3ruk, PDBj:3ruk
PDBsum3ruk
PubMed22266943
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

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