1F5V

STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1f5vb_	Alpha and beta proteins (a+b)	FMN-dependent nitroreductase-like	FMN-dependent nitroreductase-like	NADH oxidase/flavin reductase	Oxygen-insensitive NAD(P)H nitroreductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1f5va_	Alpha and beta proteins (a+b)	FMN-dependent nitroreductase-like	FMN-dependent nitroreductase-like	NADH oxidase/flavin reductase	Oxygen-insensitive NAD(P)H nitroreductase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8035417	3001947	SCOP2B (2022-06-29)
A	SCOP2 Family	NADH oxidase/flavin reductase	8023037	4001599	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FMN-dependent nitroreductase-like	8035417	3001947	SCOP2 (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	Nitroreductase	e1f5vB1	A: a+b two layers	X: Alpha-beta plaits	H: FMN-dependent nitroreductase-like (From Topology)	T: FMN-dependent nitroreductase-like	F: Nitroreductase	ECOD (1.6)
A	Nitroreductase	e1f5vA1	A: a+b two layers	X: Alpha-beta plaits	H: FMN-dependent nitroreductase-like (From Topology)	T: FMN-dependent nitroreductase-like	F: Nitroreductase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.109.10	Alpha Beta	3-Layer(aba) Sandwich	NADH Oxidase	NADH Oxidase	CATH (4.3.0)
A	3.40.109.10	Alpha Beta	3-Layer(aba) Sandwich	NADH Oxidase	NADH Oxidase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00881	Nitroreductase family (Nitroreductase)	Nitroreductase family	The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	OXYGEN-INSENSITIVE NADPH NITROREDUCTASE	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 NAD(P)H dehydrogenase (quinone) 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 NAD(P)H dehydrogenase (quinone) activity oxidoreductase activity, acting on NAD(P)H oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor catalytic activity chromate reductase activity identical protein binding protein binding protein homodimerization activity protein dimerization activity	-	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR016446	Flavin oxidoreductase Frp family	Family
A, B	IPR029479	Nitroreductase	Domain
A, B	IPR000415	Nitroreductase-like	Homologous Superfamily

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.