› 1bpq

X-ray diffraction
1.8Å resolution

PHOSPHOLIPASE A2 ENGINEERING. X-RAY STRUCTURAL AND FUNCTIONAL EVIDENCE FOR THE INTERACTION OF LYSINE-56 WITH SUBSTRATES

Released:
DOI: 10.2210/pdb1bpq/pdb
PDB entry 1bpq coloured by chain, front view.
PDB entry 1bpq coloured by chain, side view.
PDB entry 1bpq coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Phospholipase A2 engineering. X-ray structural and functional evidence for the interaction of lysine-56 with substrates.
Noel JP, Bingman CA, Deng TL, Dupureur CM, Hamilton KJ, Jiang RT, Kwak JG, Sekharudu C, Sundaralingam M, Tsai MD
Biochemistry 30 11801-11 (1991)
PMID: 1751497

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: 13.81 KDa
Source organism: Bos taurus
Expression system: Not provided
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: 45.94Å b: 45.94Å c: 102.49Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Phospholipases and their industrial applications.
De Maria et al. (2007)
4 more

2 mentions without citation

Expression, functional, and structural analysis of proteins critical for otoconia development.
Xu et al. (2010)
1 more