3ret

X-ray diffraction
1.79Å resolution

Salicylate and Pyruvate Bound Structure of the Isochorismate-Pyruvate Lyase K42E Mutant from Pseudomonas aerugionsa

Released:

Function and Biology Details

Reactions catalysed:
Isochorismate = salicylate + pyruvate
Chorismate = prephenate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-175949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isochorismate pyruvate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 101 amino acids
Theoretical weight: 11.45 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q51507 (Residues: 1-101; Coverage: 100%)
Gene names: PA4230, pchB
Sequence domains: Chorismate mutase type II
Structure domains: Chorismate mutase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 46.144Å b: 57.313Å c: 60.334Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.208 0.264
Expression system: Escherichia coli BL21(DE3)