3MZS

Crystal Structure of Cytochrome P450 CYP11A1 in complex with 22-hydroxy-cholesterol

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
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	d3mzsb_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	bovine,cow,domestic cattle,domestic cow (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
C	d3mzsc_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	bovine,cow,domestic cattle,domestic cow (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
D	d3mzsd_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	bovine,cow,domestic cattle,domestic cow (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d3mzsa_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	bovine,cow,domestic cattle,domestic cow (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	p450	e3mzsB1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
C	p450	e3mzsC1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
D	p450	e3mzsD1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
A	p450	e3mzsA1	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)
C	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
D	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00067	Cytochrome P450 (p450)	Cytochrome P450	Cytochrome P450s are haem-thiolate proteins [6] involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, a ...	Cytochrome P450s are haem-thiolate proteins [6] involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyse regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures [6].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Cholesterol side-chain cleavage enzyme	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 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen 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 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity cholesterol monooxygenase (side-chain-cleaving) activity steroid hydroxylase activity	regulation of hormone levels steroid metabolic process biological regulation C21-steroid hormone biosynthetic process lipid biosynthetic process primary metabolic process C21-steroid hormone metabolic process hormone metabolic process biosynthetic process metabolic process cellular process regulation of biological quality steroid biosynthetic process hormone biosynthetic process regulation of hormone levels steroid metabolic process biological regulation C21-steroid hormone biosynthetic process lipid biosynthetic process primary metabolic process C21-steroid hormone metabolic process hormone metabolic process biosynthetic process metabolic process cellular process regulation of biological quality steroid biosynthetic process hormone biosynthetic process steroid hormone biosynthetic process lipid metabolic process glucocorticoid metabolic process glucocorticoid biosynthetic process cellular response to nitrogen compound cellular response to stimulus response to stimulus response to endogenous stimulus response to peptide hormone cellular response to peptide hormone stimulus response to oxygen-containing compound response to nitrogen compound cellular response to oxygen-containing compound cellular response to endogenous stimulus cellular response to chemical stimulus response to hormone response to chemical cellular response to hormone stimulus fat-soluble vitamin metabolic process organic hydroxy compound metabolic process small molecule metabolic process vitamin D metabolic process vitamin metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process secondary alcohol metabolic process ketone metabolic process cortisol metabolic process olefinic compound metabolic process tertiary alcohol metabolic process primary alcohol metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050479	Cytochrome P450, families 11 and 27	Family
A, B, C, D	IPR002401	Cytochrome P450, E-class, group I	Family
A, B, C, D	IPR017972	Cytochrome P450, conserved site	Conserved Site
A, B, C, D	IPR001128	Cytochrome P450	Family
A, B, C, D	IPR036396	Cytochrome P450 superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D	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.