Function and Biology Details
Reactions catalysed:
L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H
L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH
Biochemical function:
Biological process:
Cellular component:
- not assigned
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
- Glutamate dehydrogenase
- Aminoacid dehydrogenase-like, N-terminal domain superfamily
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123099 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate dehydrogenase; NADP-specific glutamate dehydrogenase
Molecule details ›
Chains: A, B, C, D, E, F
Length: 448 amino acids
Theoretical weight: 48.43 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 448 amino acids
Theoretical weight: 48.43 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
E7GGS1 (Residues: 1-204, 408-450; Coverage: 55%) - Canonical: P00370 (Residues: 206-406; Coverage: 45%)
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:
APS BEAMLINE 24-ID-C
Spacegroup:
P1
Expression system: Escherichia coli BL21(DE3)
