PDBe 2fn1

X-ray diffraction
2.1Å resolution

Crystal structures of Yersinia enterocolitica salicylate synthase (Irp9) in complex with the reaction products salicylate and pyruvate

Released:

Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 56.571Å b: 145.298Å c: 58.86Å
α: 90° β: 108.39° γ: 90°
R-values:
R R work R free
0.191 0.188 0.245
Expression system: Escherichia coli