PDBe 4gmf

X-ray diffraction
1.85Å resolution

Apo Structure of a Thiazolinyl Imine Reductase from Yersinia enterocolitica (Irp3)

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 372 amino acids
Theoretical weight: 41.71 KDa
Source organism: Yersinia enterocolitica subsp. enterocolitica 8081
Expression system: Escherichia coli
UniProt:
  • Canonical: A1JTG0 (Residues: 2-366; Coverage: 100%)
Gene names: YE2619, ybtU
Sequence domains: Oxidoreductase family, NAD-binding Rossmann fold
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 83.871Å b: 93.903Å c: 181.121Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.242
Expression system: Escherichia coli