Function and Biology Details
Reaction catalysed:
L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, C-terminal
- NAD(P)-binding domain superfamily
- NAD(P) binding domain of glutamate dehydrogenase
- Leu/Phe/Val dehydrogenases active site
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
- Aminoacid dehydrogenase-like, N-terminal domain superfamily
- Glutamate dehydrogenase
Structure domains:
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
Glutamate dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-176345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate dehydrogenase
Molecule details ›
Chains: A, B, C, D, E, F
Length: 418 amino acids
Theoretical weight: 46.66 KDa
Source organism: Thermococcus litoralis
UniProt:
Sequence domains:
Length: 418 amino acids
Theoretical weight: 46.66 KDa
Source organism: Thermococcus litoralis
UniProt:
- Canonical:
Q56304 (Residues: 2-419; Coverage: 100%)
Sequence domains:
- Glu/Leu/Phe/Val dehydrogenase, dimerisation domain
- Glutamate/Leucine/Phenylalanine/Valine dehydrogenase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SRS BEAMLINE PX9.5
Spacegroup:
C2
