X-ray diffraction
2.25Å resolution

Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate


Function and Biology Details

Reaction catalysed:
Phosphoenolpyruvate = 3-phosphonopyruvate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Phosphoenolpyruvate phosphomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.95 KDa
Source organism: Mytilus edulis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P56839 (Residues: 1-295; Coverage: 100%)
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 90.024Å b: 130.441Å c: 90.475Å
α: 90° β: 90° γ: 90°
R R work R free
0.185 0.179 0.268
Expression system: Escherichia coli BL21(DE3)