Structure analysis

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

X-ray diffraction
2.4Å resolution
Source organism: Clostridium botulinum
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 34536.47 Å2
Buried surface area: 2716.75 Å2
Dissociation area: 1,147.61 Å2
Dissociation energy (ΔGdiss): -1.36 kcal/mol
Dissociation entropy (TΔSdiss): 14.15 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-553962

Macromolecules

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
Pfam: Clostridial neurotoxin zinc protease
InterPro: Botulinum/Tetanus toxin, catalytic chain
CATH: Metalloproteases ("zincins"), catalytic domain like

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