Function and Biology Details
Reaction catalysed:
Hydrolysis of -Gln(76)-|-Phe- bond in synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Botulinum/Tetanus toxin, catalytic chain
- Clostridium neurotoxin, translocation domain
- Kunitz inhibitor STI-like superfamily
- Clostridium neurotoxin, receptor-binding C-terminal
- Clostridium neurotoxin, receptor binding N-terminal
- Concanavalin A-like lectin/glucanase domain superfamily
- Clostridium neurotoxin, translocation
- Acetylglutamate kinase-like superfamily
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Tetanus toxin heavy chain (preferred)
PDBe Complex ID:
PDB-CPX-138291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Tetanus toxin
Molecule details ›
Chains: A, B
Length: 1335 amino acids
Theoretical weight: 152.91 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 1335 amino acids
Theoretical weight: 152.91 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P04958 (Residues: 1-1315; Coverage: 100%)
Sequence domains:
Ligands and Environments
No modified residues
Experiments and Validation Details
X-ray source:
DIAMOND BEAMLINE I04-1
Spacegroup:
P21
Expression system: Escherichia coli BL21(DE3)
