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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-134168 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Botulinum neurotoxin D light chain
Molecule details ›
Chains: A, C
Length: 453 amino acids
Theoretical weight: 51.68 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Length: 453 amino acids
Theoretical weight: 51.68 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P19321 (Residues: 1-437; Coverage: 34%)
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like
Botulinum neurotoxin D heavy chain; Somatoliberin
Molecule details ›
Chains: B, D
Length: 474 amino acids
Theoretical weight: 53.72 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Clostridium botulinum neurotoxin b, "coiled-coil" domain
Length: 474 amino acids
Theoretical weight: 53.72 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P19321 (Residues: 450-861; Coverage: 32%)
- Canonical: P01286 (Residues: 32-73; Coverage: 48%)
Sequence domains:
Structure domains: Clostridium botulinum neurotoxin b, "coiled-coil" domain
