Annotations: 4KQW

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4kqwa2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Slackia exigua ATCC 700122 ) [TaxId: 649764 ],	SCOPe (2.08)
A	d4kqwa1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Slackia exigua ATCC 700122 ) [TaxId: 649764 ],	SCOPe (2.08)
B	d4kqwb2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Slackia exigua ATCC 700122 ) [TaxId: 649764 ],	SCOPe (2.08)
B	d4kqwb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Slackia exigua ATCC 700122 ) [TaxId: 649764 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	IlvC	e4kqwA2	A: alpha arrays	X: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	H: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	T: 6-phosphogluconate dehydrogenase C-terminal domain-like	F: IlvC	ECOD (1.6)
A	IlvN	e4kqwA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: IlvN	ECOD (1.6)
B	IlvC	e4kqwB2	A: alpha arrays	X: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	H: 6-phosphogluconate dehydrogenase C-terminal domain-like (From Topology)	T: 6-phosphogluconate dehydrogenase C-terminal domain-like	F: IlvC	ECOD (1.6)
B	IlvN	e4kqwB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: IlvN	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	6.10.240.10	Special	Helix non-globular	ProC C-terminal domain-like fold		CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	6.10.240.10	Special	Helix non-globular	ProC C-terminal domain-like fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07991	Acetohydroxy acid isomeroreductase, NADPH-binding domain (IlvN)	Acetohydroxy acid isomeroreductase, NADPH-binding domain	-	Family
A, B	PF01450	Acetohydroxy acid isomeroreductase, catalytic domain (IlvC)	Acetohydroxy acid isomeroreductase, catalytic domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Ketol-acid reductoisomerase	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding oxidoreductase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding 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 ketol-acid reductoisomerase activity catalytic activity	oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process isoleucine biosynthetic process branched-chain amino acid biosynthetic process oxoacid metabolic process small molecule biosynthetic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process amino acid biosynthetic process biosynthetic process isoleucine biosynthetic process branched-chain amino acid biosynthetic process metabolic process small molecule metabolic process cellular process branched-chain amino acid metabolic process isoleucine metabolic process alpha-amino acid biosynthetic process pyruvate family amino acid metabolic process pyruvate family amino acid biosynthetic process L-amino acid biosynthetic process L-valine biosynthetic process L-amino acid metabolic process proteinogenic amino acid metabolic process proteinogenic amino acid biosynthetic process valine metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR013023	Ketol-acid reductoisomerase	Family
A, B	IPR014359	Ketol-acid reductoisomerase, prokaryotic	Family
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR000506	Ketol-acid reductoisomerase, C-terminal	Domain
A, B	IPR013116	Ketol-acid reductoisomerase, N-terminal	Domain
A, B	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain 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.