› 1aok

X-ray diffraction
2Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137397 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acidic phospholipase A2 homolog vipoxin A chain Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.66 KDa
Source organism: Vipera ammodytes meridionalis
UniProt:
  • Canonical: P04084 (Residues: 1-122; Coverage: 100%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain
Basic phospholipase A2 vipoxin B chain Chain: B
Molecule details ›
Chain: B
Length: 122 amino acids
Theoretical weight: 13.84 KDa
Source organism: Vipera ammodytes meridionalis
UniProt:
  • Canonical: P14420 (Residues: 1-122; Coverage: 100%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21212
Unit cell:
a: 67.64Å b: 67.69Å c: 46.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 0.23

Quick links

Citations

1 review citation

Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis.
Kang et al. (2011)
19 other articles

4 mentions without citation

Protein complexes in snake venom.
Doley et al. (2009)
3 more