PDBe 1pym

X-ray diffraction
1.8Å resolution

PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate phosphomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 33.28 KDa
Source organism: Mytilus edulis
Expression system: Escherichia coli
UniProt:
  • Canonical: P56839 (Residues: 1-295; Coverage: 100%)
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: C2221
Unit cell:
a: 90.4Å b: 131.1Å c: 90.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.256
Expression system: Escherichia coli