› 5u39

X-ray diffraction
1.75Å 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: 295 amino acids
Theoretical weight: 32.51 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: P47205 (Residues: 2-293; Coverage: 96%)
Gene names: PA4406, envA, lpxC
Sequence domains: UDP-3-O-acyl N-acetylglycosamine deacetylase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand C90 1 x C90
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P212121
Unit cell:
a: 35.23Å b: 82.88Å c: 87.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.202
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Pushing the envelope: LPS modifications and their consequences.
Simpson et al. (2019)
3 more

2 mentions without citation

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