3N9Y

Crystal structure of human CYP11A1 in complex with 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
Pharos: Disease Associations
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)
A	d3n9ya_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d3n9yb_	All alpha proteins	Cytochrome P450	Cytochrome P450	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d3n9yc_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d3n9yd_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	2Fe-2S ferredoxin-like	2Fe-2S ferredoxin-related	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	p450	e3n9yA1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
B	p450	e3n9yB1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
C	Fer2	e3n9yC1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: Fer2	ECOD (1.6)
D	Fer2	e3n9yD2	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: Fer2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
B	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
C	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)
D	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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	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	cellular biosynthetic process regulation of hormone levels steroid metabolic process cellular 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 cellular biosynthetic process regulation of hormone levels steroid metabolic process cellular 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 sterol metabolic process organic hydroxy compound 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 small molecule metabolic process vitamin D metabolic process vitamin metabolic process secondary alcohol metabolic process cholesterol metabolic process alcohol metabolic process cortisol metabolic process cellular ketone metabolic process olefinic compound metabolic process tertiary alcohol metabolic process primary alcohol metabolic process	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen
C, D	Adrenodoxin	iron-sulfur cluster binding 2 iron, 2 sulfur cluster binding binding metal cluster binding small molecule binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding electron transfer activity	cellular metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process regulation of hormone levels biological regulation regulation of biological quality hormone biosynthetic process hormone metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process cellular metabolic process electron transport chain metabolic process cellular process generation of precursor metabolites and energy biosynthetic process regulation of hormone levels biological regulation regulation of biological quality hormone biosynthetic process hormone metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process steroid biosynthetic process lipid metabolic process P450-containing electron transport chain secondary alcohol metabolic process organic hydroxy compound metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process small molecule metabolic process cellular response to nitrogen compound cellular response to stimulus response to stimulus response to organophosphorus cellular response to organic cyclic compound response to oxygen-containing compound response to nitrogen compound response to purine-containing compound response to cAMP cellular response to oxygen-containing compound cellular response to chemical stimulus response to chemical cellular response to cAMP response to organic cyclic compound response to ketone response to lipid response to alcohol cellular response to forskolin cellular response to alcohol response to forskolin cellular response to lipid cellular response to ketone	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle membrane-enclosed lumen mitochondrial matrix intracellular organelle lumen organelle lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050479	Cytochrome P450, families 11 and 27	Family
A, B	IPR002401	Cytochrome P450, E-class, group I	Family
A, B	IPR017972	Cytochrome P450, conserved site	Conserved Site
A, B	IPR001128	Cytochrome P450	Family
A, B	IPR036396	Cytochrome P450 superfamily	Homologous Superfamily
C, D	IPR036010	2Fe-2S ferredoxin-like superfamily	Homologous Superfamily
C, D	IPR001041	2Fe-2S ferredoxin-type iron-sulfur binding domain	Domain
C, D	IPR001055	Adrenodoxin-like	Family
C, D	IPR018298	Adrenodoxin, iron-sulphur binding site	Binding Site
C, D	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P05108	Congenital adrenal insuffiency with 46, XY sex reversal OR 46,XY disorder of sex development-adrenal insufficiency due to CYP11A1 deficiency 46,XY disorder of sex development endometrial carcinoma Adrenal Insufficiency, Congenital, With 46,Xy Sex Reversal congenital lipoid adrenal hyperplasia due to STAR deficency visual epilepsy X-linked adrenal hypoplasia congenita inherited isolated adrenal insufficiency due to partial CYP11A1 deficiency 46,XY sex reversal 3 osteoarthritis hypertensive disorder malignant ependymoma adrenocortical insufficiency pituitary cancer cleft lip Congenital adrenal insuffiency with 46, XY sex reversal OR 46,XY disorder of sex development-adrenal insufficiency due to CYP11A1 deficiency 46,XY disorder of sex development endometrial carcinoma Adrenal Insufficiency, Congenital, With 46,Xy Sex Reversal congenital lipoid adrenal hyperplasia due to STAR deficency visual epilepsy X-linked adrenal hypoplasia congenita inherited isolated adrenal insufficiency due to partial CYP11A1 deficiency 46,XY sex reversal 3 osteoarthritis hypertensive disorder malignant ependymoma adrenocortical insufficiency pituitary cancer cleft lip congenital adrenal hyperplasia endometrial cancer
C, D	Pharos: P10109	adrenal cortex carcinoma ovarian cancer ulcerative colitis heart disease pancreatic ductal adenocarcinoma myocardial infarction plasma cell myeloma

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.