5VEU

Human Cytochrome P450 3A5 (CYP3A5)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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	d5veua_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d5veub_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d5veud_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d5veue_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d5veuf_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d5veug_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d5veuh_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
J	d5veuj_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d5veuc_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
I	d5veui_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
K	d5veuk_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
L	d5veul_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
F	SCOP2 Family	Cytochrome P450	8068662	4001206	SCOP2 (2022-06-29)
F	SCOP2 Superfamily	Cytochrome P450	8068663	3001061	SCOP2 (2022-06-29)
G	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
K	SCOP2B Superfamily	Cytochrome P450	8068663	3001061	SCOP2B (2022-06-29)
L	SCOP2B Superfamily	Cytochrome P450	8068663	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)
A	p450	e5veuA1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
B	p450	e5veuB1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
D	p450	e5veuD1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
E	p450	e5veuE1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
F	p450	e5veuF1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
G	p450	e5veuG1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
H	p450	e5veuH1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
J	p450	e5veuJ1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
C	p450	e5veuC1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
I	p450	e5veuI1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
K	p450	e5veuK1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
L	p450	e5veuL1	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)
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)
D	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
E	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
F	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
G	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
H	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
J	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)
I	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
K	1.10.630.10	Mainly Alpha	Orthogonal Bundle	Cytochrome p450	Cytochrome P450	CATH (4.3.0)
L	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, E A, B, C, D, E, F, G, H, I, J, K, L	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, E A, B, C, D, E, F, G, H, I, J, K, L	Cytochrome P450 3A5	oxidoreductase activity catalytic activity estrogen 16-alpha-hydroxylase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen steroid hydroxylase activity aromatase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen oxygen binding binding small molecule binding retinoic acid 4-hydroxylase activity testosterone 6-beta-hydroxylase activity organic cyclic compound binding oxidoreductase activity catalytic activity estrogen 16-alpha-hydroxylase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen steroid hydroxylase activity aromatase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen oxygen binding binding small molecule binding retinoic acid 4-hydroxylase activity testosterone 6-beta-hydroxylase activity organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding	oxidative demethylation demethylation metabolic process cellular process lipid modification primary metabolic process lipid hydroxylation lipid metabolic process diterpenoid metabolic process oxoacid metabolic process regulation of hormone levels biological regulation carboxylic acid metabolic process organic acid metabolic process oxidative demethylation demethylation metabolic process cellular process lipid modification primary metabolic process lipid hydroxylation lipid metabolic process diterpenoid metabolic process oxoacid metabolic process regulation of hormone levels biological regulation carboxylic acid metabolic process organic acid metabolic process hormone metabolic process retinoic acid metabolic process retinoid metabolic process small molecule metabolic process regulation of biological quality monocarboxylic acid metabolic process terpenoid metabolic process isoprenoid metabolic process aflatoxin metabolic process mycotoxin metabolic process organic heteropentacyclic compound metabolic process toxin metabolic process secondary metabolic process catabolic process alkaloid catabolic process alkaloid metabolic process estrogen metabolic process steroid metabolic process cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus xenobiotic metabolic process response to xenobiotic stimulus xenobiotic catabolic process organic hydroxy compound metabolic process alcohol metabolic process olefinic compound metabolic process retinol metabolic process primary alcohol metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle intracellular membrane-bounded organelle organelle subcompartment membrane endomembrane system endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle intracellular membrane-bounded organelle organelle subcompartment membrane endomembrane system endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR008072	Cytochrome P450, E-class, CYP3A	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR002402	Cytochrome P450, E-class, group II	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR017972	Cytochrome P450, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR050705	Cytochrome P450 3A	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR001128	Cytochrome P450	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	IPR036396	Cytochrome P450 superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	Pharos: P20815	prostate cancer kidney disease essential hypertension ovarian cancer pancreatic intraductal papillary-mucinous neoplasm pituitary cancer psoriasis atypical teratoid rhabdoid tumor Thrombosis essential hypertension, genetic interstitial cystitis lung adenocarcinoma malignant glioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia prostate cancer kidney disease essential hypertension ovarian cancer pancreatic intraductal papillary-mucinous neoplasm pituitary cancer psoriasis atypical teratoid rhabdoid tumor Thrombosis essential hypertension, genetic interstitial cystitis lung adenocarcinoma malignant glioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia schizophrenia Barrett esophagus thrombotic disease toxic encephalopathy esophageal adenocarcinoma glioblastoma lung cancer malignant pancreatic neoplasm non-small cell lung carcinoma pancreatic intraductal papillary-mucinous carcinoma periodontitis cutaneous lupus erythematosus HIV infectious disease large cell medulloblastoma lung carcinoma medulloblastoma

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J, K, L	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.