› 4pk5

X-ray diffraction
2.79Å resolution

Crystal structure of the indoleamine 2,3-dioxygenagse 1 (IDO1) complexed with Amg-1

Released:
DOI: 10.2210/pdb4pk5/pdb
PDB entry 4pk5 coloured by chain, front view.
PDB entry 4pk5 coloured by chain, side view.
PDB entry 4pk5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structures and Structure-Activity Relationships of Imidazothiazole Derivatives as IDO1 Inhibitors.
Tojo S, Kohno T, Tanaka T, Kamioka S, Ota Y, Ishii T, Kamimoto K, Asano S, Isobe Y
ACS Med Chem Lett 5 1119-23 (2014)
PMID: 25313323

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Indoleamine 2,3-dioxygenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 47.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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
1 bound ligand:
Ligand PKJ 2 x PKJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 84.799Å b: 90.414Å c: 131.757Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Abnormal kynurenine pathway of tryptophan catabolism in cardiovascular diseases.
Song et al. (2017)
11 more

19 mentions without citation

Advances in indoleamine 2,3-dioxygenase 1 medicinal chemistry.
Coletti et al. (2017)
18 more