Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation

Summary for 3FFZ

DescriptorBotulinum neurotoxin type E, ZINC ION, SODIUM ION, ... (5 entities in total)
Functional Keywordsbotulinum neurotoxin serotype e, botulism, domain organization, endopeptidase, translocation, hydrolase, membrane, metal-binding, metalloprotease, neurotoxin, protease, secreted, toxin, transmembrane, zinc
Biological sourceClostridium botulinum
Cellular locationBotulinum neurotoxin E light chain: Secreted. Botulinum neurotoxin E heavy chain: Secreted Q00496
Total number of polymer chains2
Total molecular weight287910.22
Kumaran, D.,Eswaramoorthy, S.,Swaminathan, S. (deposition date: 2008-12-04, release date: 2008-12-16, Last modification date: 2011-07-13)
Primary citation
Kumaran, D.,Eswaramoorthy, S.,Furey, W.,Navaza, J.,Sax, M.,Swaminathan, S.
Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation.
J.Mol.Biol., 386:233-245, 2009
PubMed: 19118561 (PDB entries with the same primary citation)
DOI: 10.1016/j.jmb.2008.12.027
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.307294.7%8.1%5.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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