4ehx

X-ray diffraction
1.9Å resolution

Crystal structure of LpxK from Aquifex aeolicus at 1.9 angstrom resolution

Released:

Function and Biology Details

Reaction catalysed:
ATP + (2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl phosphate) = ADP + (2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-4-O-phospho-beta-D-glucosaminyl)-(1->6)-(2-N,3-O-bis((3R)-3-hydroxytetradecanoyl)-alpha-D-glucosaminyl phosphate)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetraacyldisaccharide 4'-kinase Chain: A
Molecule details ›
Chain: A
Length: 315 amino acids
Theoretical weight: 36.6 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67572 (Residues: 1-315; Coverage: 100%)
Gene names: aq_1656, lpxK
Sequence domains: Tetraacyldisaccharide-1-P 4'-kinase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 61.783Å b: 69.049Å c: 106.079Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.2
Expression system: Escherichia coli