› 6pyy

X-ray diffraction
2.4Å resolution

Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PF-06840003 in Active Site and Exo site

Released:
DOI: 10.2210/pdb6pyy/pdb
PDB entry 6pyy coloured by chain, front view.
PDB entry 6pyy coloured by chain, side view.
PDB entry 6pyy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis of Inhibitor Selectivity in Human Indoleamine 2,3-Dioxygenase 1 and Tryptophan Dioxygenase.
Pham KN, Lewis-Ballester A, Yeh SR
J Am Chem Soc 141 18771-18779 (2019)
PMID: 31682426

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
Molecule details ›
Chains: A, B, C, D
Length: 380 amino acids
Theoretical weight: 45.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48775 (Residues: 18-389; Coverage: 92%)
Gene names: TDO, TDO2
Sequence domains: Tryptophan 2,3-dioxygenase

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand H7S 8 x H7S
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21212
Unit cell:
a: 144.188Å b: 154.037Å c: 87.973Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.238
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Tryptophan: A Rheostat of Cancer Immune Escape Mediated by Immunosuppressive Enzymes IDO1 and TDO.
Kim et al. (2021)
2 more

2 mentions without citation

Structural Basis of Inhibitor Selectivity in Human Indoleamine 2,3-Dioxygenase 1 and Tryptophan Dioxygenase.
Pham et al. (2019)
1 more