› 2nox

X-ray diffraction
2.4Å resolution

Crystal structure of tryptophan 2,3-dioxygenase from Ralstonia metallidurans

Released:
DOI: 10.2210/pdb2nox/pdb
PDB entry 2nox coloured by chain, front view.
PDB entry 2nox coloured by chain, side view.
PDB entry 2nox coloured by chain, top view.
Source organism: Cupriavidus metallidurans
Primary publication:
Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis.
Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE
Biochemistry 46 145-55 (2007)
PMID: 17198384

Function and Biology Details

Reaction catalysed: 
L-tryptophan + O(2) = N-formyl-L-kynurenine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan 2,3-dioxygenase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 281 amino acids
Theoretical weight: 32.54 KDa
Source organism: Cupriavidus metallidurans
UniProt:
  • Canonical: Q1LK00 (Residues: 19-299; Coverage: 94%)
Gene names: Rmet_2651, kynA
Sequence domains: Tryptophan 2,3-dioxygenase
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments


Cofactor: Ligand HEM 16 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P1
Unit cell:
a: 72.544Å b: 132.121Å c: 139.95Å
α: 66.97° β: 85.06° γ: 89.89°
R-values:
R R work R free
0.21 0.21 0.27

Quick links

Citations

24 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
23 more

5 mentions without citation

Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase.
Fu et al. (2011)
4 more