2j65

X-ray diffraction
2.2Å resolution

Structure of LpxC from Aquifex aeolicus in complex with UDP

Released:
Source organism: Aquifex aeolicus VF5
Primary publication:
The nucleotide-binding site of Aquifex aeolicus LpxC.
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 1082-6 (2006)
PMID: 17077484

Function and Biology Details

Reaction catalysed:
UDP-3-O-((3R)-3-hydroxyacyl)-N-acetyl-alpha-D-glucosamine + H(2)O = UDP-3-O-((3R)-3-hydroxyacyl)-alpha-D-glucosamine + acetate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acyl-N-acetylglucosamine deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 271 amino acids
Theoretical weight: 30.99 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67648 (Residues: 1-271; Coverage: 96%)
Gene names: aq_1772, envA, lpxC
Sequence domains: UDP-3-O-acyl N-acetylglycosamine deacetylase
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P61
Unit cell:
a: 101.755Å b: 101.755Å c: 124.243Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.171 0.168 0.225
Expression system: Escherichia coli BL21(DE3)