› 2ok9

X-ray diffraction
2.34Å resolution

Function and Biology Details

Reaction catalysed: 
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 homolog piratoxin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 121 amino acids
Theoretical weight: 13.75 KDa
Source organism: Bothrops pirajai
UniProt:
  • Canonical: P58399 (Residues: 1-121; Coverage: 100%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

2 bound ligands:
Ligand PBP 2 x PBP
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P21
Unit cell:
a: 38.602Å b: 70.002Å c: 43.787Å
α: 90° β: 102.64° γ: 90°
R-values:
R R work R free
0.223 0.223 0.252

Quick links

Citations

4 review citations

Snake venom Lys49 myotoxins: From phospholipases A(2) to non-enzymatic membrane disruptors.
Lomonte et al. (2012)
3 more

2 mentions without citation

Structural basis for phospholipase A2-like toxin inhibition by the synthetic compound Varespladib (LY315920).
Salvador et al. (2019)
1 more