Function and Biology Details
Reaction catalysed:
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Phospholipase A2
- Pancreatic trypsin inhibitor Kunitz domain
- Phospholipase A2 domain
- Pancreatic trypsin inhibitor Kunitz domain superfamily
- Phospholipase A2 domain superfamily
- Proteinase inhibitor I2, Kunitz, conserved site
- Phospholipase A2, aspartic acid active site
- Phospholipase A2, histidine active site
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132758 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Basic phospholipase A2 beta-bungarotoxin A1 chain
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 13.52 KDa
Source organism: Bungarus multicinctus
UniProt:
Structure domains: Phospholipase A2 domain
Length: 120 amino acids
Theoretical weight: 13.52 KDa
Source organism: Bungarus multicinctus
UniProt:
- Canonical:
P00617 (Residues: 28-147; Coverage: 94%)
Structure domains: Phospholipase A2 domain
Kunitz-type serine protease inhibitor homolog beta-bungarotoxin B2 chain
Molecule details ›
Chain: B
Length: 61 amino acids
Theoretical weight: 7.21 KDa
Source organism: Bungarus multicinctus
UniProt:
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
Length: 61 amino acids
Theoretical weight: 7.21 KDa
Source organism: Bungarus multicinctus
UniProt:
- Canonical: P00989 (Residues: 25-85; Coverage: 100%)
Structure domains: Pancreatic trypsin inhibitor Kunitz domain
