X-ray diffraction
2Å resolution

Crystal structure of 4-phenylimidazole bound form of human indoleamine 2,3-dioxygenase (A260G mutant)

Source organism: Homo sapiens
Entry authors: Sugimoto H, Horitani M, Kometani E, Shiro Y

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Indoleamine 2,3-dioxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 45.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P14902 (Residues: 1-403; Coverage: 100%)
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
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 85.971Å b: 98.89Å c: 131.582Å
α: 90° β: 90° γ: 90°
R R work R free
0.188 0.186 0.231
Expression system: Escherichia coli