Annotations: 2IZ0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2iz0a2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
A	d2iz0a1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
B	d2iz0b2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
B	d2iz0b1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
B	d2iz0b3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
C	d2iz0c2	All alpha proteins	6-phosphogluconate dehydrogenase C-terminal domain-like	6-phosphogluconate dehydrogenase C-terminal domain-like	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	SCOPe (2.08)
C	d2iz0c1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	automated matches	automated matches	(Lactococcus lactis ) [TaxId: 1358 ],	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	6PGD	e2iz0A1	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: 6PGD	ECOD (1.6)
A	NAD_binding_2	e2iz0A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: NAD_binding_2	ECOD (1.6)
B	6PGD	e2iz0B1	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: 6PGD	ECOD (1.6)
B	NAD_binding_2	e2iz0B2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: NAD_binding_2	ECOD (1.6)
C	6PGD	e2iz0C1	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: 6PGD	ECOD (1.6)
C	NAD_binding_2	e2iz0C2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: NAD_binding_2	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	1.10.1040.10	Mainly Alpha	Orthogonal Bundle	N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase	domain 2	CATH (4.3.0)
A	1.20.5.320	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	6-Phosphogluconate Dehydrogenase, domain 3	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	1.10.1040.10	Mainly Alpha	Orthogonal Bundle	N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase	domain 2	CATH (4.3.0)
B	1.20.5.320	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	6-Phosphogluconate Dehydrogenase, domain 3	CATH (4.3.0)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	1.10.1040.10	Mainly Alpha	Orthogonal Bundle	N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase	domain 2	CATH (4.3.0)
C	1.20.5.320	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces	6-Phosphogluconate Dehydrogenase, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF00393	6-phosphogluconate dehydrogenase, C-terminal domain (6PGD)	6-phosphogluconate dehydrogenase, C-terminal domain	This family represents the C-terminal all-alpha domain of 6-phosphogluconate dehydrogenase. The domain contains two structural repeats of 5 helices each.	Domain
A, B, C	PF03446	NAD binding domain of 6-phosphogluconate dehydrogenase (NAD_binding_2)	NAD binding domain of 6-phosphogluconate dehydrogenase	The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding phosphogluconate dehydrogenase (decarboxylating) 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	carbohydrate metabolic process catabolic process D-gluconate catabolic process oxoacid metabolic process carbohydrate catabolic process aldonic acid catabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process organic acid catabolic process aldonic acid metabolic process cellular catabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process D-gluconate metabolic process carbohydrate metabolic process catabolic process D-gluconate catabolic process oxoacid metabolic process carbohydrate catabolic process aldonic acid catabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process organic acid catabolic process aldonic acid metabolic process cellular catabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process D-gluconate metabolic process metabolic process cellular process small molecule metabolic process monocarboxylic acid metabolic process small molecule catabolic process carbohydrate derivative metabolic process glucose 6-phosphate metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pentose-phosphate shunt pyridine-containing compound metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pentose-phosphate shunt, oxidative branch generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process NADPH regeneration organophosphate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR006115	6-phosphogluconate dehydrogenase, NADP-binding	Domain
A, B, C	IPR006114	6-phosphogluconate dehydrogenase, C-terminal	Domain
A, B, C	IPR008927	6-phosphogluconate dehydrogenase-like, C-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR006184	6-phosphogluconate-binding site	Binding Site
A, B, C	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C	IPR006113	6-phosphogluconate dehydrogenase, decarboxylating	Family
A, B, C	IPR013328	6-phosphogluconate dehydrogenase, domain 2	Homologous Superfamily
A, B, C	IPR006183	6-phosphogluconate dehydrogenase	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.