› 1eza

Solution NMR

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI NMR, RESTRAINED REGULARIZED MEAN STRUCTURE

Released:
DOI: 10.2210/pdb1eza/pdb
PDB entry 1eza coloured by chain, front view.
PDB entry 1eza coloured by chain, side view.
PDB entry 1eza coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
Biochemistry 36 2517-30 (1997)
PMID: 9054557

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate-protein phosphotransferase Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 28.38 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
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

15 review citations

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

12 mentions without citation

Protein binding site prediction using an empirical scoring function.
Liang et al. (2006)
11 more