ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE

Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography.

SEE REMARK 450 FOR INFORMATION REGARDING THE SOURCE AND SEQUENCE

DPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTE
MWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPGS
REAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEA
RRRATLLARLVGCPPGGAGGNDTELIACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDL
QVLVGVVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGD
HNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYEIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFA
RTGDPNDPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSAT

1.4 M ammonium sulfate, VAPOR DIFFUSION, temperature 298K, pH 5.5

THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO THE STRUCTURE) NOT OF ELECTROPHORUS ELECTRICUS. AT THE RESOLUTION OF THE EXPERIMENTAL DATA (4.2A) NO SEQUENCE DISCREPANCIES CAN BE SEEN

SERINE HYDROLASE, ALPHA/BETA HYDROLASE, TETRAMER, HYDROLASE