› 3bp2

X-ray diffraction
2.1Å resolution

ROLE OF THE N-TERMINUS IN THE INTERACTION OF PANCREATIC PHOSPHOLIPASE A2 WITH AGGREGATED SUBSTRATES. PROPERTIES AND CRYSTAL STRUCTURE OF TRANSAMINATED PHOSPHOLIPASE A2

Released:
DOI: 10.2210/pdb3bp2/pdb
PDB entry 3bp2 coloured by chain, front view.
PDB entry 3bp2 coloured by chain, side view.
PDB entry 3bp2 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Role of the N-terminus in the interaction of pancreatic phospholipase A2 with aggregated substrates. Properties and crystal structure of transaminated phospholipase A2.
Dijkstra BW, Kalk KH, Drenth J, de Haas GH, Egmond MR, Slotboom AJ
Biochemistry 23 2759-66 (1984)
PMID: 6466614

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: 13.81 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00593 (Residues: 24-145; Coverage: 94%)
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: P212121
Unit cell:
a: 46.68Å b: 64.85Å c: 37.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Not provided

Quick links

Citations

3 review citations

The kinetics of interfacial catalysis by phospholipase A2 and regulation of interfacial activation: hopping versus scooting.
Jain et al. (1989)
2 more

69 mentions without citation

Reprogramming cellular events by poly(ADP-ribose)-binding proteins.
Krietsch et al. (2013)
68 more