Annotations: 1BU7

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1bu7b_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	Cytochrome P450 bm-3	(Priestia megaterium ) [TaxId: 1404 ],	SCOPe (2.08)
A	d1bu7a_	All alpha proteins	Cytochrome P450	Cytochrome P450	Cytochrome P450	Cytochrome P450 bm-3	(Priestia megaterium ) [TaxId: 1404 ],	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	8039120	3001061	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Cytochrome P450	8039120	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	e1bu7B1	A: alpha arrays	X: Cytochrome P450 (From Topology)	H: Cytochrome P450 (From Topology)	T: Cytochrome P450	F: p450	ECOD (1.6)
A	p450	e1bu7A1	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)

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	PROTEIN (CYTOCHROME P450)	binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity NADPH-hemoprotein reductase activity oxidoreductase activity, acting on NAD(P)H binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding oxidoreductase activity NADPH-hemoprotein reductase activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor catalytic activity tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding metal ion binding flavin adenine dinucleotide binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen 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 identical protein binding protein binding	-	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001709	Flavoprotein pyridine nucleotide cytochrome reductase	Domain
A, B	IPR001433	Oxidoreductase FAD/NAD(P)-binding	Domain
A, B	IPR003097	Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding	Domain
A, B	IPR023173	NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain superfamily	Homologous Superfamily
A, B	IPR023206	Bifunctional cytochrome P450/NADPH--cytochrome P450 reductase	Family
A, B	IPR008254	Flavodoxin/nitric oxide synthase	Domain
A, B	IPR039261	Ferredoxin-NADP reductase (FNR), nucleotide-binding domain	Homologous Superfamily
A, B	IPR017972	Cytochrome P450, conserved site	Conserved Site
A, B	IPR017938	Riboflavin synthase-like beta-barrel	Homologous Superfamily
A, B	IPR001094	Flavodoxin-like	Domain
A, B	IPR001128	Cytochrome P450	Family
A, B	IPR017927	FAD-binding domain, ferredoxin reductase-type	Domain
A, B	IPR029039	Flavoprotein-like superfamily	Homologous Superfamily
A, B	IPR036396	Cytochrome P450 superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
B	cytochrome P450 (BM-3) M-CSA #699	Cytochromes P450, a gene superfamily of heme proteins found in all eukaryotes, most prokaryotes, and Archaea, catalyse the mono-oxygenation of a wide variety of organic molecules. P450 reactions of biological significance include steroid bio-genesis, drug metabolism, procarcinogen activation, xenobiotic detoxification, and fatty acid metabolism. P450BM-3 consists of heme (BMP) and FMN/FAD containing reductase domains linked together by a single polypeptide.	Defined by 3 residues: THR:B-268PHE:B-393CYS:B-400 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.14.14.1 (PDB Primary Data) Search M-CSA Motif + EC 1.14.14.1 EC: 1.6.2.4 (UniProt) Search M-CSA Motif + EC 1.6.2.4

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.