X-ray diffraction
1.45Å resolution

NADP+ bound structure of Irp3, a Thiazolinyl Imine Reductase from Yersinia enterocolitica


Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Gfo/Idh/MocA-like oxidoreductase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 385 amino acids
Theoretical weight: 42.93 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O54512 (Residues: 1-365; Coverage: 100%)
Gene name: irp3
Sequence domains: Oxidoreductase family, NAD-binding Rossmann fold
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 41.444Å b: 148.506Å c: 65.006Å
α: 90° β: 95.62° γ: 90°
R R work R free
0.16 0.159 0.179
Expression system: Escherichia coli BL21(DE3)