› 2yvw

X-ray diffraction
1.81Å resolution

Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Aquifex aeolicus VF5

Released:
DOI: 10.2210/pdb2yvw/pdb
PDB entry 2yvw coloured by chain, front view.
PDB entry 2yvw coloured by chain, side view.
PDB entry 2yvw coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Entry authors: Kitamuta Y, Yokoyama S, Kuramitsu S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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-130482 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chain: A
Molecule details ›
Chain: A
Length: 425 amino acids
Theoretical weight: 47.32 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67315 (Residues: 1-425; Coverage: 100%)
Gene names: aq_1281, murA
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

2 bound ligands:
Ligand PO4 1 x PO4
Ligand EPU 1 x EPU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P62
Unit cell:
a: 132.004Å b: 132.004Å c: 58.165Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.22
Expression system: Escherichia coli

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