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
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-209623 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Botulinum neurotoxin A light chain
Molecule details ›
Chain: B
Length: 252 amino acids
Theoretical weight: 28.36 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Length: 252 amino acids
Theoretical weight: 28.36 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
- Canonical:
P0DPI1 (Residues: 3-250; Coverage: 19%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Botulinum neurotoxin A light chain
Molecule details ›
Chain: C
Length: 175 amino acids
Theoretical weight: 20.62 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains:
Length: 175 amino acids
Theoretical weight: 20.62 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
- Canonical: P0DPI1 (Residues: 251-425; Coverage: 14%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains:
