› 3bk9

X-ray diffraction
2.15Å resolution

H55A mutant of tryptophan 2,3-dioxygenase from Xanthomonas campestris

Released:
DOI: 10.2210/pdb3bk9/pdb
PDB entry 3bk9 coloured by chain, front view.
PDB entry 3bk9 coloured by chain, side view.
PDB entry 3bk9 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: 306 amino acids
Theoretical weight: 35.66 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 13 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 78.222Å b: 117.606Å c: 139.283Å
α: 90° β: 95.73° γ: 90°
R-values:
R R work R free
0.205 0.2 0.285
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

1 mention without citation

A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study.
Shin et al. (2021)