5ZCM

Crystal structure of Xylose reductase from Debaryomyces nepalensis in complex with NADP-DTT adduct

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	d5zcma1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	NAD(P)-linked oxidoreductase	Aldo-keto reductases (NADP)	automated matches	(Debaryomyces nepalensis ) [TaxId: 27299 ],	SCOPe (2.08)
A	d5zcma2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Debaryomyces nepalensis ) [TaxId: 27299 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	NAD(P)-linked oxidoreductase	8062025	3000288	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)
A	Aldo_ket_red	e5zcmA1	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	Aldose reductase	aldo-keto reductase (NADPH) activity alcohol dehydrogenase [NAD(P)+] 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 alcohol dehydrogenase (NADP+) activity D-xylose reductase (NADPH) activity catalytic activity aldose reductase (NADPH) activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding aldo-keto reductase (NADPH) activity alcohol dehydrogenase [NAD(P)+] 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 alcohol dehydrogenase (NADP+) activity D-xylose reductase (NADPH) activity catalytic activity aldose reductase (NADPH) activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	monosaccharide metabolic process carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process D-xylose metabolic process D-xylose catabolic process small molecule metabolic process metabolic process monosaccharide catabolic process small molecule catabolic process pentose metabolic process pentose catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR018170	Aldo/keto reductase, conserved site	Conserved Site
A	IPR036812	NADP-dependent oxidoreductase domain superfamily	Homologous Superfamily
A	IPR044486	Aldo-keto reductase family 2B	Family
A	IPR023210	NADP-dependent oxidoreductase domain	Domain
A	IPR020471	Aldo-keto reductase	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.