› 1s2v

X-ray diffraction
2.1Å resolution

Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)

Released:
DOI: 10.2210/pdb1s2v/pdb
PDB entry 1s2v coloured by chain, front view.
PDB entry 1s2v coloured by chain, side view.
PDB entry 1s2v 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

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157568 (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:
Ligand MG 4 x MG
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)

Quick links

Citations

8 citation in other articles

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
7 more

1 mention without citation

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