4e75

X-ray diffraction
2.85Å resolution

Structure of LpxD from Acinetobacter baumannii at 2.85A resolution (P21 form)

Released:
Source organism: Acinetobacter baumannii

Function and Biology Details

Reaction catalysed:
A (3R)-3-hydroxyacyl-[acyl-carrier-protein] + a UDP-3-O-((3R)-hydroxyacyl)-alpha-D-glucosamine = a UDP-2-N,3-O-bis((3R)-3-hydroxyacyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-109251 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acylglucosamine N-acyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 357 amino acids
Theoretical weight: 38.47 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli
UniProt:
  • Canonical: B0VMV2 (Residues: 2-355; Coverage: 99%)
Gene names: ABSDF1688, lpxD
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 106.679Å b: 209.614Å c: 107.633Å
α: 90° β: 119.23° γ: 90°
R-values:
R R work R free
0.237 0.234 0.28
Expression system: Escherichia coli