1s2u

X-ray diffraction
2Å resolution

Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein

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

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-157568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate phosphomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 295 amino acids
Theoretical weight: 32.91 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: C2221
Unit cell:
a: 108.537Å b: 119.746Å c: 88.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.165 0.219
Expression system: Escherichia coli BL21(DE3)