› 3uhm

X-ray diffraction
1.26Å resolution

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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-3-O-acyl-N-acetylglucosamine deacetylase Chain: A
Molecule details ›
Chain: A
Length: 299 amino acids
Theoretical weight: 33.15 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P47205 (Residues: 1-299; Coverage: 99%)
Gene names: PA4406, envA, lpxC
Sequence domains: UDP-3-O-acyl N-acetylglycosamine deacetylase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand RFN 1 x RFN
Ligand GAI 1 x GAI
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 34.138Å b: 80.965Å c: 49.779Å
α: 90° β: 95.5° γ: 90°
R-values:
R R work R free
0.181 0.18 0.201
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
9 more

3 mentions without citation

Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer.
Clayton et al. (2013)
2 more