› 1vap

X-ray diffraction
1.6Å resolution

THE MONOMERIC ASP49 SECRETORY PHOSPHOLIPASE A2 FROM THE VENOM OF AGKISTRIDON PISCIVORUS PISCIVORUS

Released:
DOI: 10.2210/pdb1vap/pdb
PDB entry 1vap coloured by chain, front view.
PDB entry 1vap coloured by chain, side view.
PDB entry 1vap coloured by chain, top view.
Source organism: Agkistrodon piscivorus piscivorus
Primary publication:
Structural aspects of interfacial adsorption. A crystallographic and site-directed mutagenesis study of the phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus.
Han SK, Yoon ET, Scott DL, Sigler PB, Cho W
J Biol Chem 272 3573-82 (1997)
PMID: 9013608

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156442 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 APP-D49 Chains: A, B
Molecule details ›
Chains: A, B
Length: 123 amino acids
Theoretical weight: 14.01 KDa
Source organism: Agkistrodon piscivorus piscivorus
UniProt:
  • Canonical: P51972 (Residues: 1-123; Coverage: 100%)
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 34.71Å b: 39.89Å c: 42.85Å
α: 94.17° β: 79.1° γ: 106.27°
R-values:
R R work R free
0.197 0.197 not available

Quick links

Citations

14 review citations

Biochemistry and physiology of mammalian secreted phospholipases A2.
Lambeau et al. (2008)
13 more

4 mentions without citation

The role of hydrophobic interactions in positioning of peripheral proteins in membranes.
Lomize et al. (2007)
3 more