› 1s2w

X-ray diffraction
1.69Å resolution

Crystal structure of phosphoenolpyruvate mutase in high ionic strength

Released:
DOI: 10.2210/pdb1s2w/pdb
PDB entry 1s2w coloured by chain, front view.
PDB entry 1s2w coloured by chain, side view.
PDB entry 1s2w coloured by chain, top view.
Source organism: Mytilus edulis
Primary publication:
Conformational flexibility of PEP mutase.
Liu S, Lu Z, Han Y, Jia Y, Howard A, Dunaway-Mariano D, Herzberg O
Biochemistry 43 4447-53 (2004)
PMID: 15078090

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate = 3-phosphonopyruvate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-157566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate phosphomutase Chain: A
Molecule details ›
Chain: A
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:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: C2221
Unit cell:
a: 76.632Å b: 116.556Å c: 72.818Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.178 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.
Lyagin et al. (2021)
8 other articles

1 mention without citation

'Hot' macromolecular crystals.
Koclega et al. (2009)