Structure of PDB 5irq Chain A

Receptor sequence
>5irqA (length=466) Species: 9606 (Homo sapiens) [Search protein sequence]
LLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQ
LAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMA
TFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVIS
LICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLE
KLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNDSELL
SDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVG
FSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVD
KGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGA
GPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLID
SFKVKIKVRQAWREAQ
3D structure
PDB5irq Structural and Functional Evaluation of Clinically Relevant Inhibitors of Steroidogenic Cytochrome P450 17A1.
ChainA
Resolution2.202 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 A R96 I112 A113 R125 A302 G303 T306 V366 L370 I371 H373 P434 F435 R440 C442 I443 G444 R66 I82 A83 R95 A265 G266 T269 V329 L333 I334 H336 P397 F398 R403 C405 I406 G407
BS02 6D7 A Y201 N202 G301 A302 Y171 N172 G264 A265 BindingDB: IC50=38nM
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:5irq, PDBe:5irq, PDBj:5irq
PDBsum5irq
PubMed28373265
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

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