› 4p2p

X-ray diffraction
2.4Å resolution

AN INDEPENDENT CRYSTALLOGRAPHIC REFINEMENT OF PORCINE PHOSPHOLIPASE A2 AT 2.4 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb4p2p/pdb
PDB entry 4p2p coloured by chain, front view.
PDB entry 4p2p coloured by chain, side view.
PDB entry 4p2p coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution.
Finzel BC, Ohlendorf DH, Weber PC, Salemme FR
Acta Crystallogr B 47 ( Pt 4) 558-9 (1991)
PMID: 1930837

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132749 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2, major isoenzyme Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 14.01 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P00592 (Residues: 23-146; Coverage: 95%)
Gene name: PLA2G1B
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 69.4Å b: 69.4Å c: 70.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 not available not available
Expression system: Not provided

Quick links

Citations

7 citation in other articles

Knowledge-based interaction potentials for proteins.
Rojnuckarin et al. (1999)
6 more

2 mentions without citation

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