X-ray diffraction
1.25Å resolution

LpxC from A.Aaeolicus in complex with 4-[[4-[2-[4-(morpholinomethyl)phenyl]ethynyl]phenoxy]methyl]tetrahydropyran-4-carbohydroxamic acid (compound 9)

Source organism: Aquifex aeolicus VF5
Entry author: Olivier NB

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
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
UDP-3-O-acyl-N-acetylglucosamine deacetylase Chain: A
Molecule details ›
Chain: A
Length: 271 amino acids
Theoretical weight: 30.99 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli BL21(DE3)
  • 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: APS BEAMLINE 17-ID
Spacegroup: P61
Unit cell:
a: 65.865Å b: 65.865Å c: 133.282Å
α: 90° β: 90° γ: 120°
R R work R free
0.158 0.158 0.168
Expression system: Escherichia coli BL21(DE3)