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TitleThe X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 118, Page 2340-2346, Year 1996
Publish dateFeb 13, 1996 (structure data deposition date)
AuthorsHarel, M. / Quinn, D.M. / Nair, H.K. / Silman, I. / Sussman, J.L.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.8 Å
Structure data

PDB-1amn:
TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-NAF:
M-(N,N,N-TRIMETHYLAMMONIO)-2,2,2-TRIFLUORO-1,1-DIHYDROXYETHYLBENZENE

ChemComp-HOH:
WATER

Source
  • torpedo californica (Pacific electric ray)
KeywordsHYDROLASE (SERINE ESTERASE) / HYDROLASE / SERINE ESTERASE / SYNAPSE / MEMBRANE / NERVE / MUSCLE / NEUROTRANSMITTER DEGRADATION / GLYCOPROTEIN / GPI-ANCHOR / ALTERNATIVE SPLICING

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