› 2d0u

X-ray diffraction
3.4Å resolution

Crystal structure of cyanide bound form of human indoleamine 2,3-dioxygenase

Released:
DOI: 10.2210/pdb2d0u/pdb
PDB entry 2d0u coloured by chain, front view.
PDB entry 2d0u coloured by chain, side view.
PDB entry 2d0u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.
Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y
Proc Natl Acad Sci U S A 103 2611-6 (2006)
PMID: 16477023

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147133 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indoleamine 2,3-dioxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 45.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • 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:
Ligand CYN 2 x CYN
Ligand NHE 4 x NHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 86.352Å b: 97.089Å c: 129.378Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.249 0.213 0.254
Expression system: Escherichia coli

Quick links

Citations

61 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
60 more

11 mentions without citation

AhR-Mediated, Non-Genomic Modulation of IDO1 Function.
Pallotta et al. (2014)
10 more