Function and Biology Details
Reactions catalysed:
(S)-malate + NAD(+) = oxaloacetate + NADH
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH
Sequence domains:
- D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site
- D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1
- D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain
- NAD(P)-binding domain superfamily
- D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
D-3-phosphoglycerate dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-128865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-3-phosphoglycerate dehydrogenase
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 33.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 314 amino acids
Theoretical weight: 33.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O43175 (Residues: 4-315; Coverage: 59%)
Sequence domains:
