X-ray diffraction
1.4Å resolution

Crystal structure of PagP in SDS/MPD


Function and Biology Details

Reaction catalysed:
1-palmitoyl-2-acyl-sn-glycero-3-phosphocholine + hexa-acyl lipid A = 2-acyl-sn-glycero-3-phosphocholine + hepta-acyl lipid A
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Lipid A palmitoyltransferase PagP Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 19.24 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
  • Canonical: P37001 (Residues: 26-186; Coverage: 100%)
Gene names: JW0617, b0622, crcA, pagP, ybeG
Sequence domains: Antimicrobial peptide resistance and lipid A acylation protein PagP
Structure domains: Porin

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6222
Unit cell:
a: 113.228Å b: 113.228Å c: 55.064Å
α: 90° β: 90° γ: 120°
R R work R free
0.173 0.171 0.208
Expression system: Escherichia coli