› 4bp2

X-ray diffraction
1.6Å resolution

CRYSTALLOGRAPHIC REFINEMENT OF BOVINE PRO-PHOSPHOLIPASE A2 AT 1.6 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb4bp2/pdb
PDB entry 4bp2 coloured by chain, front view.
PDB entry 4bp2 coloured by chain, side view.
PDB entry 4bp2 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystallographic refinement of bovine pro-phospholipase A2 at 1.6 A resolution.
Finzel BC, Weber PC, Ohlendorf DH, Salemme FR
Acta Crystallogr., B 47 ( Pt 5) 814-6 (1991)
PMID: 1793547

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-132750 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.54 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00593 (Residues: 16-145; Coverage: 100%)
Gene name: PLA2G1B
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand MPD 2 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 46.95Å b: 46.95Å c: 102Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

4 citation in other articles

Structural elements of secretory phospholipases A2 involved in the binding to M-type receptors.
Lambeau et al. (1995)
3 more

5 mentions without citation

Do all backbone polar groups in proteins form hydrogen bonds?
Fleming et al. (2005)
4 more