5xe1

X-ray diffraction
3.2Å resolution

Crystal structure of the indoleamine 2,3-dioxygenagse 1 (IDO1) complexed with INCB14943

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights into the binding mechanism of IDO1 with hydroxylamidine based inhibitor INCB14943.
Biochem Biophys Res Commun 487 339-343 (2017)
PMID: 28412361

Function and Biology Details

Reaction catalysed:
D-tryptophan + O(2) = N-formyl-D-kynurenine
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer
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: 403 amino acids
Theoretical weight: 45.38 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P212121
Unit cell:
a: 87.05Å b: 97.38Å c: 128.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.274
Expression system: Escherichia coli BL21(DE3)