› 3e08

X-ray diffraction
1.9Å resolution

H55S mutant Xanthomonas campestris tryptophan 2,3-dioxygenase

Released:
DOI: 10.2210/pdb3e08/pdb
PDB entry 3e08 coloured by chain, front view.
PDB entry 3e08 coloured by chain, side view.
PDB entry 3e08 coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris
Primary publication:
Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.
Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK
Biochemistry 47 10677-84 (2008)
PMID: 18783250

Function and Biology Details

Reaction catalysed: 
L-tryptophan + O(2) = N-formyl-L-kynurenine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 2,3-dioxygenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 298 amino acids
Theoretical weight: 34.61 KDa
Source organism: Xanthomonas campestris pv. campestris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8PDA8 (Residues: 1-298; Coverage: 100%)
Gene names: XCC0432, kynA
Sequence domains: Tryptophan 2,3-dioxygenase
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments


Cofactor: Ligand HEM 8 x HEM
1 bound ligand:
Ligand TRP 16 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 77.912Å b: 117.718Å c: 138.978Å
α: 90° β: 95.64° γ: 90°
R-values:
R R work R free
0.178 0.178 0.216
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Control of immune response by amino acid metabolism.
Grohmann et al. (2010)
6 more