› 1yxw

X-ray diffraction
2.2Å resolution

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

Released:
DOI: 10.2210/pdb1yxw/pdb
PDB entry 1yxw coloured by chain, front view.
PDB entry 1yxw coloured by chain, side view.
PDB entry 1yxw coloured by chain, top view.
Source organism: Clostridium tetani
Primary publication:
Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin.
Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S
Proteins 61 288-95 (2005)
PMID: 16104015

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:
Sequence domains:
Structure domains:

Structure analysis Details

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

Ligands and Environments

3 bound ligands:
Ligand TYR 1 x TYR
Ligand GLU 1 x GLU
Ligand TRP 1 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 66.757Å b: 79.183Å c: 90.265Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.274

Quick links

Citations

10 review citations

Gangliosides in cell recognition and membrane protein regulation.
Lopez et al. (2009)
9 more