› 5zbd

X-ray diffraction
1.8Å resolution

Crystal structure of tryptophan oxidase (C395A mutant) from Chromobacterium violaceum

Released:
DOI: 10.2210/pdb5zbd/pdb
PDB entry 5zbd coloured by chain, front view.
PDB entry 5zbd coloured by chain, side view.
PDB entry 5zbd coloured by chain, top view.
Source organism: Chromobacterium violaceum ATCC 12472
Primary publication:
Protein engineering for improving the thermostability of tryptophan oxidase and insights from structural analysis.
Yamaguchi H, Tatsumi M, Takahashi K, Tagami U, Sugiki M, Kashiwagi T, Kameya M, Okazaki S, Mizukoshi T, Asano Y
J Biochem 164 359-367 (2018)
PMID: 30053101

Function and Biology Details

Reaction catalysed: 
7-chloro-L-tryptophan + O(2) = 2-imino-3-(7-chloroindol-3-yl)propanoate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent L-tryptophan oxidase VioA Chains: A, B
Molecule details ›
Chains: A, B
Length: 451 amino acids
Theoretical weight: 50.48 KDa
Source organism: Chromobacterium violaceum ATCC 12472
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9S3V1 (Residues: 1-418; Coverage: 100%)
Gene names: CV_3274, vioA
Sequence domains: Flavin containing amine oxidoreductase

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand TRP 2 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 87.86Å b: 89.27Å c: 112.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Catalytic mechanism of ancestral L-lysine oxidase assigned by sequence data mining.
Sugiura et al. (2021)
1 more

2 mentions without citation

Recent Advances in Synthetic, Industrial and Biological Applications of Violacein and Its Heterologous Production.
Ahmed et al. (2021)
1 more