› 1zym

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate-protein phosphotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 28.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08839 (Residues: 1-258; Coverage: 45%)
Gene names: JW2409, b2416, ptsI
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 47.42Å b: 75.78Å c: 170.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.306
Expression system: Escherichia coli

Quick links

Citations

12 review citations

How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
Deutscher et al. (2006)
11 more

18 mentions without citation

Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization.
Clore GM. (2000)
17 more