Function and Biology Details
Reactions catalysed:
(S)-malate + NAD(+) = oxaloacetate + NADH
3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Malate dehydrogenase, type 2
- Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal
- Malate dehydrogenase, NAD-dependent, cytosolic
- Lactate/malate dehydrogenase, C-terminal
- Malate dehydrogenase, active site
- Lactate/malate dehydrogenase, N-terminal
- NAD(P)-binding domain superfamily
- L-lactate/malate dehydrogenase
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Malate dehydrogenase, cytoplasmic (preferred)
PDBe Complex ID:
PDB-CPX-154206 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase, cytoplasmic
Molecule details ›
Chains: A, B
Length: 334 amino acids
Theoretical weight: 36.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 334 amino acids
Theoretical weight: 36.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P40925 (Residues: 1-334; Coverage: 100%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
APS BEAMLINE 17-ID
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
