1s2v

X-ray diffraction
2.1Å resolution

Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)

Released:
Source organism: Mytilus edulis
Primary publication:
Conformational flexibility of PEP mutase.
Biochemistry 43 4447-53 (2004)
PMID: 15078090

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
Macromolecule:
Phosphoenolpyruvate phosphomutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 295 amino acids
Theoretical weight: 32.95 KDa
Source organism: Mytilus edulis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56839 (Residues: 1-295; Coverage: 100%)
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P21212
Unit cell:
a: 122.517Å b: 86.469Å c: 104.011Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.257
Expression system: Escherichia coli BL21(DE3)