CATH Domain 2g76A02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.50	Rossmann fold
	3.40.50.720	NAD(P)-binding Rossmann-like Domain

Domain Context

CATH Clusters

Superfamily	NAD(P)-binding Rossmann-like Domain
Functional Family	D-3-phosphoglycerate dehydrogenase

Enzyme Information

1.1.1.37	Malate dehydrogenase. based on mapping to UniProt O43175 (S)-malate + NAD(+) = oxaloacetate + NADH. -!- Also oxidizes some other 2-hydroxydicarboxylic acids.
1.1.1.399	2-oxoglutarate reductase. based on mapping to UniProt O43175 (R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH. -!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.
1.1.1.95	Phosphoglycerate dehydrogenase. based on mapping to UniProt O43175 3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH. -!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.

UniProtKB Entries (1)

SERA_HUMAN

Homo sapiens

D-3-phosphoglycerate dehydrogenase

PDB Structure

PDB	2G76
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure of human 3-phosphoglycerate dehydrogenase Turnbull, A.P., Salah, E., Savitsky, P., Gileadi, O., von Delft, F., Edwards, A., Arrowsmith, C., Weigelt, J., Sundstrom, M., Oppermann, U. To be Published