1mkt

X-ray diffraction
1.72Å resolution

CARBOXYLIC ESTER HYDROLASE, 1.72 ANGSTROM TRIGONAL FORM OF THE BOVINE RECOMBINANT PLA2 ENZYME

Released:
Source organism: Bos taurus
Primary publication:
1.72 A resolution refinement of the trigonal form of bovine pancreatic phospholipase A2.
Acta Crystallogr D Biol Crystallogr 54 342-6 (1998)
PMID: 9761901

Function and Biology Details

Reaction catalysed:
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.81 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00593 (Residues: 23-145; Coverage: 95%)
Gene name: PLA2G1B
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU R-AXIS II
Spacegroup: P3121
Unit cell:
a: 46.78Å b: 46.78Å c: 102.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.284
Expression system: Escherichia coli