› 6cxv

X-ray diffraction
2.6Å resolution

Structure of the S167H mutant of human indoleamine 2,3 dioxygenase in complex with tryptophan and cyanide

Released:
DOI: 10.2210/pdb6cxv/pdb
PDB entry 6cxv coloured by chain, front view.
PDB entry 6cxv coloured by chain, side view.
PDB entry 6cxv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1.
Lewis-Ballester A, Karkashon S, Batabyal D, Poulos TL, Yeh SR
J Am Chem Soc 140 8518-8525 (2018)
PMID: 29897749

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:
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: 425 amino acids
Theoretical weight: 47.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14902 (Residues: 11-403; Coverage: 98%)
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
3 bound ligands:
Ligand CYN 2 x CYN
Ligand TRP 2 x TRP
Ligand ZCW 2 x ZCW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 88.66Å b: 98.09Å c: 126.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.266
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Indoleamine 2,3-dioxygenase 1 (IDO1): an up-to-date overview of an eclectic immunoregulatory enzyme.
Pallotta et al. (2022)
1 more

1 mention without citation

Inhibition Mechanisms of Human Indoleamine 2,3 Dioxygenase 1.
Lewis-Ballester et al. (2018)