2R96

Crystal structure of E. coli WrbA in complex with FMN

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 [auth C]	d2r96c_	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	WrbA-like	Trp repressor binding protein WrbA	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d2r96a_	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	WrbA-like	Trp repressor binding protein WrbA	(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 [auth C]	SCOP2B Superfamily	Flavoproteins	8066681	3001217	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Flavoproteins	8066681	3001217	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 [auth C]	FMN_red	e2r96C1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: FMN_red	ECOD (1.6)
A	FMN_red	e2r96A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: Flavoproteins	F: FMN_red	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth C]	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)
A	3.40.50.360	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Flavodoxin domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C]	PF03358	NADPH-dependent FMN reductase (FMN_red)	NADPH-dependent FMN reductase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C]	Flavoprotein WrbA	oxidoreductase activity NADH:ubiquinone reductase (non-electrogenic) activity oxidoreductase activity, acting on NAD(P)H catalytic activity oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor NADH dehydrogenase activity binding nucleotide binding FMN binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding oxidoreductase activity NADH:ubiquinone reductase (non-electrogenic) activity oxidoreductase activity, acting on NAD(P)H catalytic activity oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor NADH dehydrogenase 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 purine nucleotide binding adenyl nucleotide binding NADP binding flavin adenine dinucleotide binding NAD(P)H dehydrogenase (quinone) activity NADPH dehydrogenase (quinone) activity NAD binding identical protein binding protein binding	response to oxidative stress response to stimulus response to stress	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C]	IPR010089	Flavoprotein WrbA-like	Family
A, B [auth C]	IPR005025	NADPH-dependent FMN reductase-like domain	Domain
A, B [auth C]	IPR008254	Flavodoxin/nitric oxide synthase	Domain
A, B [auth C]	IPR037513	NAD(P)H dehydrogenase (quinone), prokaryotic	Family
A, B [auth C]	IPR029039	Flavoprotein-like superfamily	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.