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Discovery of a novel and selective IDO-1 inhibitor PF-06840003 and its characterization as a potential clinical candidate.

X-ray diffraction
2.28Å resolution
PDB entry 5whr coloured by chain, front view.
PDB entry 5whr coloured by chain, side view.
PDB entry 5whr coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Indoleamine 2,3-dioxygenase 1
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Multimeric state: homo dimer
Accessible surface area: 30049.96 Å2
Buried surface area: 3741.6 Å2
Dissociation area: 616.37 Å2
Dissociation energy (ΔGdiss): -9.27 kcal/mol
Dissociation entropy (TΔSdiss): 13.98 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-147134

Macromolecules

Indoleamine 2,3-dioxygenase 1
Chains: A, B
Length: 393 amino acids
Theoretical weight: 44.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Best match: P14902 (Residues: 12-403)
Gene names: IDO, IDO1, INDO
Indoleamine 2,3-dioxygenase 1 in PDB entry 5whr, assembly 1, front view.
Indoleamine 2,3-dioxygenase 1 in PDB entry 5whr, assembly 1, side view.
Indoleamine 2,3-dioxygenase 1 in PDB entry 5whr, assembly 1, top view.
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