Structure of PDB 6wr0 Chain C

Receptor sequence
>6wr0C (length=474) Species: 9606 (Homo sapiens) [Search protein sequence]
SLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHH
QLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAM
ATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVI
SLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTL
EKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAG
PDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLY
EEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDS
SIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPS
VSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGI
PKVVFLIDSFKVKIKVRQAWREAQ
3D structure
PDB6wr0 Human cytochrome P450 17A1 structures with metabolites of prostate cancer drug abiraterone reveal substrate-binding plasticity and a second binding site.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T306 F435 C442
Catalytic site (residue number reindexed from 1) T277 F406 C413
Enzyme Commision number 1.14.14.19: steroid 17alpha-monooxygenase.
1.14.14.32: 17alpha-hydroxyprogesterone deacetylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM C R96 I112 R125 A302 T306 V366 L370 I371 H373 P434 F435 R440 C442 I443 A448 R67 I83 R96 A273 T277 V337 L341 I342 H344 P405 F406 R411 C413 I414 A419
BS02 U7P C A113 N202 D298 A302 T306 V482 A84 N173 D269 A273 T277 V453 BindingDB: IC50=6.1nM
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6wr0, PDBe:6wr0, PDBj:6wr0
PDBsum6wr0
PubMed36773804
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

[Back to BioLiP]