5wmv

X-ray diffraction
2.6Å resolution

Structural Insights into Substrate and Inhibitor Binding Sites in Human Indoleamine 2,3-Dioxygenase 1

Released:

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)
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: 47.79 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 89.092Å b: 97.705Å c: 127.108Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.26
Expression system: Escherichia coli