› 4pw8

X-ray diffraction
2.9Å resolution

Human tryptophan 2,3-dioxygenase

Released:
DOI: 10.2210/pdb4pw8/pdb
PDB entry 4pw8 coloured by chain, front view.
PDB entry 4pw8 coloured by chain, side view.
PDB entry 4pw8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analyses of human tryptophan 2,3-dioxygenase.
Meng B, Wu D, Gu J, Ouyang S, Ding W, Liu ZJ
Proteins 82 3210-6 (2014)
PMID: 25066423

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-155809 (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: 373 amino acids
Theoretical weight: 44.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48775 (Residues: 19-388; Coverage: 91%)
Gene names: TDO, TDO2
Sequence domains: Tryptophan 2,3-dioxygenase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 134.334Å b: 156.922Å c: 160.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.222
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The kynurenine pathway and neurodegenerative disease.
Maddison et al. (2015)
7 more

1 mention without citation

Identification of an evolutionary conserved structural loop that is required for the enzymatic and biological function of tryptophan 2,3-dioxygenase.
Michels et al. (2016)