Function and Biology Details
Reaction catalysed:
L-tryptophan + NAD(P)(+) = (indol-3-yl)pyruvate + NH(3) + NAD(P)H
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
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, bacterial/archaeal
- NAD(P)-binding domain superfamily
- Leu/Phe/Val dehydrogenases active site
- Glutamate/phenylalanine/leucine/valine/L-tryptophan dehydrogenase, dimerisation domain
- Aminoacid dehydrogenase-like, N-terminal domain superfamily
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
L-tryptophan dehydrogenase (preferred)
PDBe Complex ID:
PDB-CPX-197787 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-tryptophan dehydrogenase
Molecule details ›
Chains: A, B, C, D, E, F
Length: 361 amino acids
Theoretical weight: 39.59 KDa
Source organism: Nostoc punctiforme NIES-2108
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 361 amino acids
Theoretical weight: 39.59 KDa
Source organism: Nostoc punctiforme NIES-2108
Expression system: Escherichia coli
UniProt:
- Canonical:
W8CV45 (Residues: 1-353; 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:
PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup:
P21
Expression system: Escherichia coli
