› 5ti9

X-ray diffraction
2.5Å resolution

Crystal structure of human TDO in complex with Trp and dioxygen, Northeast Structural Genomics Consortium Target HR6161

Released:
DOI: 10.2210/pdb5ti9/pdb
PDB entry 5ti9 coloured by chain, front view.
PDB entry 5ti9 coloured by chain, side view.
PDB entry 5ti9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase.
Lewis-Ballester A, Forouhar F, Kim SM, Lew S, Wang Y, Karkashon S, Seetharaman J, Batabyal D, Chiang BY, Hussain M, Correia MA, Yeh SR, Tong L
Sci Rep 6 35169 (2016)
PMID: 27762317

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
4 bound ligands:
Ligand OXY 2 x OXY
Ligand TRP 6 x TRP
Ligand PO4 2 x PO4
Ligand NFK 2 x NFK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P21212
Unit cell:
a: 143.601Å b: 154.009Å c: 87.801Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.159 0.23
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Role of IDO and TDO in Cancers and Related Diseases and the Therapeutic Implications.
Ye et al. (2019)
7 more

8 mentions without citation

Rejigging Electron and Proton Transfer to Transition between Dioxygenase, Monooxygenase, Peroxygenase, and Oxygen Reduction Activity: Insights from Bioinspired Constructs of Heme Enzymes.
Mukherjee et al. (2021)
7 more