Function and Biology Details
Reaction catalysed:
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
- Malate dehydrogenase, type 1
- Lactate/malate dehydrogenase, C-terminal
- Malate dehydrogenase, active site
- NAD(P)-binding domain superfamily
- Malate dehydrogenase, type 1, bacterial
- L-lactate/malate dehydrogenase
- Lactate/malate dehydrogenase, N-terminal
Structure domains:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Malate dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-158430 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase
Molecule details ›
Chains: A, C, E, G
Length: 312 amino acids
Theoretical weight: 32.37 KDa
Source organism: Escherichia coli K-12
UniProt:
Sequence domains:
Length: 312 amino acids
Theoretical weight: 32.37 KDa
Source organism: Escherichia coli K-12
UniProt:
- Canonical:
P61889 (Residues: 1-312; Coverage: 100%)
Sequence domains:
- lactate/malate dehydrogenase, NAD binding domain
- lactate/malate dehydrogenase, alpha/beta C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SRS BEAMLINE PX10.1
Spacegroup:
C2
