› 3kr6

X-ray diffraction
1.7Å 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-141532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 44.87 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A749 (Residues: 1-419; Coverage: 100%)
Gene names: JW3156, b3189, murA, murZ
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

2 bound ligands:
Ligand FFQ 1 x FFQ
Ligand UD1 1 x UD1
1 modified residue:
Ligand IAS 1 x IAS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 64.4Å b: 61.8Å c: 134.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 0.188
Expression system: Escherichia coli

Quick links

Citations

9 review citations

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

5 mentions without citation

The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) .
Han et al. (2010)
4 more