› 1mks

X-ray diffraction
1.9Å resolution

CARBOXYLIC ESTER HYDROLASE, TRIGONAL FORM OF THE TRIPLE MUTANT

Released:
DOI: 10.2210/pdb1mks/pdb
PDB entry 1mks coloured by chain, front view.
PDB entry 1mks coloured by chain, side view.
PDB entry 1mks coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99.
Sekar K, Yu BZ, Rogers J, Lutton J, Liu X, Chen X, Tsai MD, Jain MK, Sundaralingam M
Biochemistry 36 3104-14 (1997)
PMID: 9115986

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: 123 amino acids
Theoretical weight: 13.78 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

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 47.08Å b: 47.08Å c: 102.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Quorum-quenching microbial infections: mechanisms and implications.
Dong et al. (2007)
4 more

2 mentions without citation

3dSS: 3D structural superposition.
Sumathi et al. (2006)
1 more