› 1naw

X-ray diffraction
2Å 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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152536 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chains: A, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand HAI 2 x HAI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2
Unit cell:
a: 86.9Å b: 155.9Å c: 83.85Å
α: 90° β: 91.65° γ: 90°
R-values:
R R work R free
0.197 0.197 0.27
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
9 more

5 mentions without citation

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
4 more