› 1m1b

X-ray diffraction
2.25Å resolution

Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate

Released:
DOI: 10.2210/pdb1m1b/pdb
PDB entry 1m1b coloured by chain, front view.
PDB entry 1m1b coloured by chain, side view.
PDB entry 1m1b coloured by chain, top view.
Source organism: Mytilus edulis
Primary publication:
Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants.
Liu S, Lu Z, Jia Y, Dunaway-Mariano D, Herzberg O
Biochemistry 41 10270-6 (2002)
PMID: 12162742

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
Molecule details ›
Chains: A, B
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

2 bound ligands:
Ligand MG 2 x MG
Ligand SPV 2 x SPV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 90.024Å b: 130.441Å c: 90.475Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.179 0.268
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Biosynthesis of phosphonic and phosphinic acid natural products.
Metcalf et al. (2009)
3 more

1 mention without citation

Coupling between catalytic loop motions and enzyme global dynamics.
Kurkcuoglu et al. (2012)