1g9c

X-ray diffraction
2.35Å resolution

CRYSTAL STRUCTURE OF CLOSTRIDIUM BOTULINUM NEUROTOXIN B COMPLEXED WITH AN INHIBITOR (EXPERIMENT 4)

Released:
Source organism: Clostridium botulinum
Primary publication:
A novel mechanism for Clostridium botulinum neurotoxin inhibition.
Biochemistry 41 9795-802 (2002)
PMID: 12146945

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 74.73Å b: 122.47Å c: 94.25Å
α: 90° β: 112.67° γ: 90°
R-values:
R R work R free
0.21 0.21 0.247