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 domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-144073 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin A light chain
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 48.56 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Length: 424 amino acids
Theoretical weight: 48.56 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli
UniProt:
- Canonical:
P0DPI1 (Residues: 2-420; Coverage: 32%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Synaptosomal-associated protein 25
Molecule details ›
Chain: B
Length: 59 amino acids
Theoretical weight: 6.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Length: 59 amino acids
Theoretical weight: 6.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P60880 (Residues: 146-204; Coverage: 29%)
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces
