7a62

X-ray diffraction
2.44Å resolution

Structure of human indoleamine-2,3-dioxygenase 1 (hIDO1) with a complete JK loop

Released:
Source organism: Homo sapiens
Primary publication:
Influence of the presence of the heme cofactor on the JK-loop structure in indoleamine 2,3-dioxygenase 1.
Acta Crystallogr D Struct Biol 76 1211-1221 (2020)
PMID: 33263327

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, 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 BL21(DE3)
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21212
Unit cell:
a: 80.96Å b: 117.95Å c: 216.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.257
Expression system: Escherichia coli BL21(DE3)