› 1kvy

X-ray diffraction
1.9Å resolution

CARBOXYLIC ESTER HYDROLASE, SINGLE MUTANT D49E COORDINATED TO CALCIUM

Released:
DOI: 10.2210/pdb1kvy/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1kvy coloured by chain, front view.
PDB entry 1kvy coloured by chain, side view.
PDB entry 1kvy coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structures of the catalytic site mutants D99A and H48Q and the calcium-loop mutant D49E of phospholipase A2.
Sekar K, Biswas R, Li Y, Tsai M, Sundaralingam M
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
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-132751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.82 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:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU R-AXIS II
Spacegroup: P3121
Unit cell:
a: 46.87Å b: 46.87Å c: 103.04Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.277
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Active-site mutagenesis of a Lys49-phospholipase A2: biological and membrane-disrupting activities in the absence of catalysis.
Ward et al. (2002)
5 more

2 mentions without citation

Rapid catalytic template searching as an enzyme function prediction procedure.
Nilmeier et al. (2013)
1 more