8QPO

E. coli NfsB with the unnatural amino acid p-nitrophenylalanine at position 124.

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	FMN-dependent nitroreductase-like	8034655	3001947	SCOP2B (2022-06-29)

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	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, C, D, E A, B, C, D, E, F, G, H	Oxygen-insensitive NAD(P)H 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 identical protein binding protein binding protein homodimerization activity 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 identical protein binding protein binding protein homodimerization activity protein dimerization activity 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 oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors 6,7-dihydropteridine reductase activity oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor oxidoreductase activity, acting on other nitrogenous compounds as donors	2,4,6-trinitrotoluene catabolic process catabolic process benzene-containing compound metabolic process trinitrotoluene metabolic process nitrotoluene catabolic process trinitrotoluene catabolic process toluene-containing compound metabolic process 2,4,6-trinitrotoluene metabolic process metabolic process cellular process nitrotoluene metabolic process toluene-containing compound catabolic process	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029479	Nitroreductase	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR033878	Oxygen-insensitive NAD(P)H nitroreductase NfsB-like	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR050627	Nitroreductase/BluB	Family
A, B, C, D, E A, B, C, D, E, F, G, H	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.