› 5whr

X-ray diffraction
2.28Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indoleamine 2,3-dioxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 393 amino acids
Theoretical weight: 44.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14902 (Residues: 12-403; Coverage: 97%)
Gene names: IDO, IDO1, INDO
Sequence domains: Indoleamine 2,3-dioxygenase
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
1 bound ligand:
Ligand AOJ 2 x AOJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 85.2Å b: 91.99Å c: 131.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Reimagining IDO Pathway Inhibition in Cancer Immunotherapy via Downstream Focus on the Tryptophan-Kynurenine-Aryl Hydrocarbon Axis.
Labadie et al. (2019)
9 more

4 mentions without citation

Indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors in clinical trials for cancer immunotherapy.
Tang et al. (2021)
3 more