5jat

X-ray diffraction
2.04Å resolution

Exploitation of a Novel Binding Pocket in Human Lipoprotein-Associated Phospholipase A2 (Lp-PLA2) Discovered Through X-Ray Fragment Screening

Released:

Function and Biology Details

Reaction catalysed:
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171527 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Platelet-activating factor acetylhydrolase Chain: A
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 44.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13093 (Residues: 46-428; Coverage: 91%)
Gene names: PAFAH, PLA2G7
Sequence domains: Platelet-activating factor acetylhydrolase, isoform II
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 100.06Å b: 91.067Å c: 51.442Å
α: 90° β: 111.72° γ: 90°
R-values:
R R work R free
0.142 0.14 0.199
Expression system: Escherichia coli