1zl6

X-ray diffraction
2.4Å resolution

Crystal structure of Tyr350Ala mutant of Clostridium botulinum neurotoxin E catalytic domain

Released:

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-169427 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Botulinum neurotoxin E light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 420 amino acids
Theoretical weight: 47.6 KDa
Source organism: Clostridium botulinum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q00496 (Residues: 2-421; Coverage: 34%)
Gene name: botE
Sequence domains: Clostridial neurotoxin zinc protease
Structure domains: Metalloproteases ("zincins"), catalytic domain like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 88.8Å b: 144.958Å c: 83.185Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.284
Expression system: Escherichia coli BL21(DE3)