2QX4

Crystal Structure of Quinone Reductase II

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2qx4b_	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	Quinone reductase	Quinone reductase type 2 (menadione reductase)	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2qx4a_	Alpha and beta proteins (a/b)	Flavodoxin-like	Flavoproteins	Quinone reductase	Quinone reductase type 2 (menadione reductase)	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)
B	SCOP2B Superfamily	Flavoproteins	8036466	3001217	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Flavoproteins	8036466	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	FMN_red	e2qx4B1	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	e2qx4A1	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	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	PF02525	Flavodoxin-like fold (Flavodoxin_2)	Flavodoxin-like fold	This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cell ...	This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyse the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species [1]. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy [1]. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP [2]. This family is related to Pfam:PF03358 and Pfam:PF00258.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ribosyldihydronicotinamide dehydrogenase [quinone]	oxidoreductase activity catalytic activity oxidoreductase activity, acting on other nitrogenous compounds as donors binding organic cyclic compound binding resveratrol binding identical protein binding protein binding protein homodimerization activity protein dimerization activity oxidoreductase activity, acting on diphenols and related substances as donors dihydronicotinamide riboside quinone reductase activity FAD binding flavin adenine dinucleotide binding oxidoreductase activity catalytic activity oxidoreductase activity, acting on other nitrogenous compounds as donors binding organic cyclic compound binding resveratrol binding identical protein binding protein binding protein homodimerization activity protein dimerization activity oxidoreductase activity, acting on diphenols and related substances as donors dihydronicotinamide riboside quinone reductase activity FAD binding flavin adenine dinucleotide binding nucleoside phosphate binding ion binding anion binding nucleotide binding heterocyclic compound binding small molecule binding melatonin binding amide binding 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 cation binding transition metal ion binding zinc ion binding metal ion binding electron transfer activity chloride ion binding	catabolic process ketone metabolic process ketone catabolic process quinone catabolic process metabolic process cellular process small molecule metabolic process small molecule catabolic process quinone metabolic process	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol nucleus extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR003680	Flavodoxin-like fold	Domain
A, B	IPR029039	Flavoprotein-like superfamily	Homologous Superfamily
A, B	IPR051545	NAD(P)H dehydrogenase (quinone)	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P16083	agranulocytosis bone marrow disease contact dermatitis Liver Cirrhosis, Experimental breast carcinoma large cell medulloblastoma astrocytic tumor pancreatic ductal adenocarcinoma chronic eosinophilic leukemia pilocytic astrocytoma schizophrenia vitiligo hypertensive disorder nephrosclerosis B-cell chronic lymphocytic leukemia agranulocytosis bone marrow disease contact dermatitis Liver Cirrhosis, Experimental breast carcinoma large cell medulloblastoma astrocytic tumor pancreatic ductal adenocarcinoma chronic eosinophilic leukemia pilocytic astrocytoma schizophrenia vitiligo hypertensive disorder nephrosclerosis B-cell chronic lymphocytic leukemia osteosarcoma breast cancer primary myelofibrosis systemic mastocytosis gastrointestinal stromal tumor idiopathic hypereosinophilic syndrome medulloblastoma non-small cell lung carcinoma ovarian cancer dermatofibrosarcoma protuberans ulcerative colitis hereditary breast carcinoma

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.