1yyn

X-ray diffraction
2.3Å resolution

A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-138291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Tetanus toxin heavy chain Chain: A
Molecule details ›
Chain: A
Length: 441 amino acids
Theoretical weight: 50.48 KDa
Source organism: Clostridium tetani
Expression system: Escherichia coli
UniProt:
  • Canonical: P04958 (Residues: 875-1315; Coverage: 34%)
Gene names: CTC_p60, tetX
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLA, SIA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 70.907Å b: 78.93Å c: 90.977Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.255 0.288
Expression system: Escherichia coli