4j1l

X-ray diffraction
2.6Å resolution

Mutant Endotoxin TeNT

Released:
Source organism: Clostridium tetani E88
Primary publication:
Engineering Clostridia Neurotoxins with elevated catalytic activity.
Toxicon 74 158-66 (2013)
PMID: 23994593

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tetanus toxin light chain Chain: A
Molecule details ›
Chain: A
Length: 426 amino acids
Theoretical weight: 49.06 KDa
Source organism: Clostridium tetani E88
Expression system: Escherichia coli
UniProt:
  • Canonical: P04958 (Residues: 2-427; Coverage: 32%)
Gene names: CTC_p60, tetX
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C222
Unit cell:
a: 105.38Å b: 176.83Å c: 57.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.238 0.266
Expression system: Escherichia coli