4R21

Zebra fish cytochrome P450 17A2 with Progesterone

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d4r21b_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	(Danio rerio ) [TaxId: 7955 ],	SCOPe (2.08)
A	d4r21a_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	(Danio rerio ) [TaxId: 7955 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Cytochrome P450	8068647	3001061	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cytochrome P450	8068647	3001061	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	p450	e4r21B1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
A	p450	e4r21A1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
A	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Cytochrome P450 family 17 polypeptide 2	oxidoreductase activity monooxygenase activity steroid 17-alpha-monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity steroid hydroxylase activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding oxidoreductase activity monooxygenase activity steroid 17-alpha-monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity steroid hydroxylase activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding	ketone metabolic process regulation of hormone levels steroid metabolic process biological regulation primary metabolic process C21-steroid hormone metabolic process hormone metabolic process progesterone metabolic process olefinic compound metabolic process metabolic process cellular process regulation of biological quality lipid metabolic process biosynthetic process ketone metabolic process regulation of hormone levels steroid metabolic process biological regulation primary metabolic process C21-steroid hormone metabolic process hormone metabolic process progesterone metabolic process olefinic compound metabolic process metabolic process cellular process regulation of biological quality lipid metabolic process biosynthetic process hormone biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR017972	Cytochrome P450, conserved site	Conserved Site
A, B	IPR002401	Cytochrome P450, E-class, group I	Family
A, B	IPR001128	Cytochrome P450	Family
A, B	IPR036396	Cytochrome P450 superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM				Cytochrome P450

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.