Structure of PDB 5irv Chain B

Receptor sequence
>5irvB (length=471) Species: 9606 (Homo sapiens) [Search protein sequence]
LLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQ
LAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMA
TFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLE
KLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGPDQD
SELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEID
QNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGE
FAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYL
PFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVV
FLIDSFKVKIKVRQAWREAQA
3D structure
PDB5irv Structural and Functional Evaluation of Clinically Relevant Inhibitors of Steroidogenic Cytochrome P450 17A1.
ChainB
Resolution3.098 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) T273 F402 C409
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 B R96 I112 A113 R125 I299 G303 V366 L370 I371 H373 F435 R440 C442 I443 A448 R66 I82 A83 R95 I266 G270 V333 L337 I338 H340 F402 R407 C409 I410 A415
BS02 6D8 B A105 F114 I205 I206 R239 G301 A302 T306 I371 V482 A75 F84 I175 I176 R209 G268 A269 T273 I338 V449 BindingDB: IC50=170nM
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:5irv, PDBe:5irv, PDBj:5irv
PDBsum5irv
PubMed28373265
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

[Back to BioLiP]