3H4G

Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor Fidarestat: Implications for inhibitor binding and selectivity

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)
A	d3h4ga_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	NAD(P)-linked oxidoreductase	Aldo-keto reductases (NADP)	Aldose reductase (aldehyde reductase)	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Aldo-keto reductases (NADP)	8061998	4003124	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	NAD(P)-linked oxidoreductase	8061999	3000288	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)
A	Aldo_ket_red	e3h4gA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Aldo_ket_red	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.100	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	NADP-dependent oxidoreductase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00248	Aldo/keto reductase family (Aldo_ket_red)	Aldo/keto reductase family	This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Alcohol dehydrogenase [NADP+]	methylglyoxal reductase (NADPH) (acetol producing) activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity glycerol dehydrogenase [NAD(P)+] activity glycerol dehydrogenase (NADP+) activity aldo-keto reductase (NADPH) activity alcohol dehydrogenase [NAD(P)+] activity alcohol dehydrogenase (NADP+) activity aldose reductase (NADPH) activity glucuronolactone reductase activity S-nitrosoglutathione reductase (NADPH) activity allyl-alcohol dehydrogenase activity methylglyoxal reductase (NADPH) (acetol producing) activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity glycerol dehydrogenase [NAD(P)+] activity glycerol dehydrogenase (NADP+) activity aldo-keto reductase (NADPH) activity alcohol dehydrogenase [NAD(P)+] activity alcohol dehydrogenase (NADP+) activity aldose reductase (NADPH) activity glucuronolactone reductase activity S-nitrosoglutathione reductase (NADPH) activity allyl-alcohol dehydrogenase activity L-glucuronate reductase activity	cellular response to stimulus cellular detoxification response to stimulus detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to toxic substance cellular detoxification of aldehyde cellular response to chemical stimulus cellular response to aldehyde response to chemical cellular process cellular response to toxic substance catabolic process cellular response to stimulus cellular detoxification response to stimulus detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to toxic substance cellular detoxification of aldehyde cellular response to chemical stimulus cellular response to aldehyde response to chemical cellular process cellular response to toxic substance catabolic process oxoacid metabolic process uronic acid metabolic process cellular metabolic process carboxylic acid metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process monocarboxylic acid catabolic process D-glucuronate catabolic process glucuronate metabolic process carboxylic acid catabolic process small molecule metabolic process metabolic process monocarboxylic acid metabolic process small molecule catabolic process D-glucuronate metabolic process glucuronate catabolic process cellular aldehyde metabolic process aldehyde catabolic process primary metabolic process lipid metabolic process monosaccharide metabolic process cellular biosynthetic process vitamin biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process L-ascorbic acid metabolic process lactone biosynthetic process water-soluble vitamin metabolic process carbohydrate metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process carbohydrate biosynthetic process monosaccharide biosynthetic process vitamin metabolic process biosynthetic process lactone metabolic process L-ascorbic acid biosynthetic process	cell periphery apical part of cell membrane plasma membrane plasma membrane region cellular anatomical entity apical plasma membrane intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018170	Aldo/keto reductase, conserved site	Conserved Site
A	IPR020471	Aldo-keto reductase	Family
A	IPR036812	NADP-dependent oxidoreductase domain superfamily	Homologous Superfamily
A	IPR023210	NADP-dependent oxidoreductase domain	Domain
A	IPR044481	Aldo-keto reductase family 1 member A1	Family

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.