› 3kqa

X-ray diffraction
2.25Å resolution

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 419 amino acids
Theoretical weight: 44.83 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli
UniProt:
  • Canonical: P33038 (Residues: 1-419; Coverage: 100%)
Gene names: ECL_04571, murA, murZ
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

2 bound ligands:
Ligand TR9 4 x TR9
Ligand CA 10 x CA
1 modified residue:
Ligand IAS 4 x IAS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 115.27Å b: 115.27Å c: 277.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.254
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structural perspective of peptidoglycan biosynthesis and assembly.
Lovering et al. (2012)
8 more

4 mentions without citation

Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).
Zhu et al. (2012)
3 more