Structure of PDB 6ww0 Chain C Binding Site BS02

Receptor Information
>6ww0 Chain C (length=467) 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
KLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDQDSELL
SDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVG
FSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVD
KGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGA
GPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLID
SFKVKIKVRQAWREAQA
Ligand information
Ligand IDUDJ
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/h3-4,7,13,15,17,19,21-22H,5-6,8-12,14H2,1-2H3/t17-,19-,21-,22-,23-,24+/m0/s1
InChIKeyFKNZCFYWNHCQGE-IRMBCWQZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7CC12CCC(=O)CC1CCC3C2CCC4(C3CC=C4c5cccnc5)C
CACTVS 3.385C[C@]12CCC(=O)C[C@@H]1CC[C@@H]3[C@@H]2CC[C@@]4(C)[C@H]3CC=C4c5cccnc5
CACTVS 3.385C[C]12CCC(=O)C[CH]1CC[CH]3[CH]2CC[C]4(C)[CH]3CC=C4c5cccnc5
ACDLabs 12.01c1ccncc1C=4C3(CCC5C2(CCC(=O)CC2CCC5C3CC=4)C)C
OpenEye OEToolkits 2.0.7C[C@]12CCC(=O)C[C@@H]1CC[C@@H]3[C@@H]2CC[C@]4([C@H]3CC=C4c5cccnc5)C
FormulaC24 H31 N O
Name(5alpha,8alpha)-17-(pyridin-3-yl)androst-16-en-3-one
ChEMBL
DrugBank
ZINCZINC000003797551
PDB chain6ww0 Chain C Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6ww0 Human cytochrome P450 17A1 structures with metabolites of prostate cancer drug abiraterone reveal substrate-binding plasticity and a second binding site.
Resolution2.01 Å
Binding residue
(original residue number in PDB)		A113 N202 I205 I206 A302 T306
Binding residue
(residue number reindexed from 1)		A83 N172 I175 I176 A265 T269
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T306 F435 C442
Catalytic site (residue number reindexed from 1) T269 F398 C405
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

View graph for
Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6ww0, PDBe:6ww0, PDBj:6ww0
PDBsum6ww0
PubMed36773804
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

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