X-ray diffraction
1.9Å resolution

Crystal structure analysis of LpxA, a UDP-N-acetylglucosamine acyltransferase from Bacteroides fragilis 9343


Function and Biology Details

Reaction catalysed:
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D-glucosamine = an [acyl-carrier-protein] + a UDP-3-O-(3-hydroxyacylyl)-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
UDP N-acetylglucosamine O-acyltransferase C-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 29.91 KDa
Source organism: Bacteroides fragilis NCTC 9343
Expression system: Escherichia coli
  • Canonical: Q5LH16 (Residues: 1-255; Coverage: 100%)
Gene names: BF9343_0789, NCTC9343_02447, lpxA, lpxA_2
Sequence domains: Udp N-acetylglucosamine O-acyltransferase; Domain 2
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P4132
Unit cell:
a: 149.051Å b: 149.051Å c: 149.051Å
α: 90° β: 90° γ: 90°
R R work R free
0.157 0.155 0.192
Expression system: Escherichia coli