1kvx

X-ray diffraction
1.9Å resolution

CARBOXYLIC ESTER HYDROLASE, SINGLE MUTANT D99A OF BOVINE PANCREATIC PLA2, 1.9 A ORTHORHOMBIC FORM

Released:
Source organism: Bos taurus
Primary publication:
Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.
Acta Crystallogr. D Biol. Crystallogr. 55 443-7 (1999)
PMID: 10089353

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.77 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: P212121
Unit cell:
a: 46.56Å b: 64.57Å c: 37.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.313
Expression system: Escherichia coli