› 6e45

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF HUMAN INDOLEAMINE 2,3-DIOXYGENASE 1 (IDO1) free enzyme in the ferrous state

Released:
DOI: 10.2210/pdb6e45/pdb
PDB entry 6e45 coloured by chain, front view.
PDB entry 6e45 coloured by chain, side view.
PDB entry 6e45 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution structures of inhibitor complexes of human indoleamine 2,3-dioxygenase 1 in a new crystal form.
Luo S, Xu K, Xiang S, Chen J, Chen C, Guo C, Tong Y, Tong L
Acta Crystallogr F Struct Biol Commun 74 717-724 (2018)
PMID: 30387777

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 405 amino acids
Theoretical weight: 45.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14902 (Residues: 15-403; Coverage: 97%)
Gene names: IDO, IDO1, INDO
Sequence domains: Indoleamine 2,3-dioxygenase

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
2 bound ligands:
Ligand GOL 5 x GOL
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2
Spacegroup: P21212
Unit cell:
a: 79.969Å b: 196.538Å c: 116.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.226
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

4 mentions without citation

High-resolution structures of inhibitor complexes of human indoleamine 2,3-dioxygenase 1 in a new crystal form.
Luo et al. (2018)
3 more