2nw7

X-ray diffraction
2.7Å resolution

Crystal Structure of Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris in complex with ferric heme. Northeast Structural Genomics Target XcR13

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-185742 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 2,3-dioxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 306 amino acids
Theoretical weight: 35.73 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 4 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 88.939Å b: 109.359Å c: 125.513Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.257 0.263
Expression system: Escherichia coli