PDBe 2fn0

X-ray diffraction
1.85Å resolution

Crystal structure of Yersinia enterocolitica salicylate synthase (Irp9)


Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Salicylate synthetase, Irp9 Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 48.31 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli
  • Canonical: Q9X9I8 (Residues: 1-434; Coverage: 100%)
Gene name: irp9
Sequence domains: chorismate binding enzyme
Structure domains: Anthranilate synthase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 56.74Å b: 145.671Å c: 58.807Å
α: 90° β: 107.97° γ: 90°
R R work R free
0.19 0.187 0.24
Expression system: Escherichia coli