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
Assembly composition:
hetero dimer (preferred)
Assembly name:
Botulinum neurotoxin type B (preferred)
PDBe Complex ID:
PDB-CPX-145486 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin B light chain
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 52.29 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Length: 453 amino acids
Theoretical weight: 52.29 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P10844 (Residues: 1-437; Coverage: 34%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Botulinum neurotoxin B heavy chain
Molecule details ›
Chain: B
Length: 433 amino acids
Theoretical weight: 49.76 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Clostridium neurotoxin, Translocation domain
Structure domains: Clostridium botulinum neurotoxin b, "coiled-coil" domain
Length: 433 amino acids
Theoretical weight: 49.76 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P10844 (Residues: 446-858; Coverage: 32%)
Sequence domains: Clostridium neurotoxin, Translocation domain
Structure domains: Clostridium botulinum neurotoxin b, "coiled-coil" domain
