1T3C

Clostridium botulinum type E catalytic domain E212Q mutant

Summary for 1T3C

• Entry DOI: 10.2210/pdb1t3c/pdb
• Related: 1T3A
• Descriptor: neurotoxin type E, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: clostridium botulinum, catalytic domain, e212q mutant, light chain, hydrolase, toxin
• Biological source: Clostridium botulinum
• Cellular location: Botulinum neurotoxin E light chain: Secreted. Botulinum neurotoxin E heavy chain: Secreted: Q00496
• Total number of polymer chains: 2
• Total formula weight: 95889.71

Authors

Agarwal, R.,Eswaramoorthy, S.,Kumaran, D.,Binz, T.,Swaminathan, S. (deposition date: 2004-04-26, release date: 2004-06-29, Last modification date: 2023-08-23)

• Primary citation: Agarwal, R.,Eswaramoorthy, S.,Kumaran, D.,Binz, T.,Swaminathan, S.; Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway; Biochemistry, 43:6637-6644, 2004; PubMed: 15157097; DOI: 10.1021/bi036278w

Experimental method

X-RAY DIFFRACTION (1.9 Å)