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Structure paper

TitleAnalysis of Active Site Residues of Botulinum Neurotoxin E by Mutational, Functional, and Structural Studies: Glu335Gln Is an Apoenzyme.
Journal, issue, pagesBiochemistry, Vol. 44, Page 8291-8302, Year 2005
Publish dateMay 4, 2005 (structure data deposition date)
AuthorsAgarwal, R. / Binz, T. / Swaminathan, S.
External linksBiochemistry / PubMed:15938619
MethodsX-ray diffraction
Resolution2.17 - 2.6 Å
Structure data

PDB-1zkw:
Crystal structure of Arg347Ala mutant of botulinum neurotoxin E catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.17 Å

PDB-1zkx:
Crystal structure of Glu158Ala/Thr159Ala/Asn160Ala- a triple mutant of Clostridium botulinum neurotoxin E catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.52 Å

PDB-1zl5:
Crystal structure of Glu335Gln mutant of Clostridium botulinum neurotoxin E catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-1zl6:
Crystal structure of Tyr350Ala mutant of Clostridium botulinum neurotoxin E catalytic domain
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1zn3:
Crystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type E
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • clostridium botulinum (bacteria)
KeywordsHYDROLASE / botulinum neurotoxin E / Arg347Ala mutant / catalytic domain / light chain / Glu158Ala/Thr159Ala/Asn160Ala mutant / Glu335Gln mutant / apoenzyme / Tyr350Ala mutant / Glu335Ala mutant

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