Function and Biology Details
Reaction catalysed:
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domain:
Structure domain:
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Botulinum neurotoxin A2 light chain (preferred)
PDBe Complex ID:
PDB-CPX-175084 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin A2 light chain
Molecule details ›
Chains: A, C
Length: 287 amino acids
Theoretical weight: 32.15 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Length: 287 amino acids
Theoretical weight: 32.15 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q45894 (Residues: 5-250; Coverage: 19%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Botulinum neurotoxin A2 light chain
Molecule details ›
Chains: B, D
Length: 174 amino acids
Theoretical weight: 20.56 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains:
Length: 174 amino acids
Theoretical weight: 20.56 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical: Q45894 (Residues: 251-416; Coverage: 13%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains:
