PDBe 5kvs

X-ray diffraction
1.28Å resolution

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

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Yersiniabactin biosynthetic protein YbtU 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)
UniProt:
  • Canonical: A0A0T9SSV9 (Residues: 2-366; Coverage: 100%)
Gene names: ERS137951_03705, irp3
Sequence domains: Oxidoreductase family, NAD-binding Rossmann fold
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 41.389Å b: 148.553Å c: 65.396Å
α: 90° β: 95.3° γ: 90°
R-values:
R R work R free
0.162 0.162 0.174
Expression system: Escherichia coli BL21(DE3)