eF-site ID 1mah-AF PDB Code 1mah Chain A, F click to enlarge Title FASCICULIN2-MOUSE ACETYLCHOLINESTERASE COMPLEX Classification COMPLEX (HYDROLASE/TOXIN) Compound ACETYLCHOLINESTERASE Source ORGANISM_COMMON: eastern green mamba; ORGANISM_SCIENTIFIC: Dendroaspis angusticeps; Sequence A:  EDPQLLVRVRGGQLRGIRLKAPGGPVSAFLGIPFAEPPVG SRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGT EMWNPNRELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGF YSGAASLDVYDGRFLAQVEGAVLVSMNYRVGTFGFLALPG SREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGES AGAASVGMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGE ARRRATLLARLVGCNDTELIACLRTRPAQDLVDHEWHVLP QESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVGV VKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQA SDLAAEAVVLHYTDWLHPEDPTHLRDAMSAVVGDHNVVCP VAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGYE IEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPN DPRDSKSPQWPPYTTAAQQYVSLNLKPLEVRRGLRAQTCA FWNRFLPKLLSAT F:  TMCYSHTTTSRAILTNCGENSCYRKSRRHPPKMVLGRGCG CPPGDDNLEVKCCTSPDKCNY Description (1)  ACETYLCHOLINESTERASE, FASCICULIN 2 Functional site 1) chain A residue 203 type sequence S description LOCATED AT THE BOTTOM OF A NARROW GORGE source : CAT 2) chain A residue 334 type sequence E description LOCATED AT THE BOTTOM OF A NARROW GORGE source : CAT 3) chain A residue 447 type sequence H description LOCATED AT THE BOTTOM OF A NARROW GORGE source : CAT 4) chain A residue 86 type sequence W description LOCATED AT THE BOTTOM OF A NARROW GORGE source : CAT 5) chain A residue 72 type sequence Y description BINDING SITE FOR FAS2 LOOP II source : PAS 6) chain A residue 124 type sequence Y description BINDING SITE FOR FAS2 LOOP II source : PAS 7) chain A residue 279 type sequence Q description BINDING SITE FOR FAS2 LOOP II source : PAS 8) chain A residue 341 type sequence Y description BINDING SITE FOR FAS2 LOOP II source : PAS 9) chain A residue 121 type catalytic sequence G description 922 source MCSA : MCSA1 10) chain A residue 122 type catalytic sequence G description 922 source MCSA : MCSA1 11) chain A residue 203 type catalytic sequence S description 922 source MCSA : MCSA1 12) chain A residue 204 type catalytic sequence A description 922 source MCSA : MCSA1 13) chain A residue 295 type catalytic sequence F description 922 source MCSA : MCSA1 14) chain A residue 334 type catalytic sequence E description 922 source MCSA : MCSA1 15) chain A residue 338 type catalytic sequence F description 922 source MCSA : MCSA1 16) chain A residue 447 type catalytic sequence H description 922 source MCSA : MCSA1 17) chain A residue 190-205 type prosite sequence FGGDPMSVTLFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpmsVtLfGeSAG source prosite : PS00122 18) chain F residue 38-56 type prosite sequence GCGCPPGDDNLEVKCCTSP description SNAKE_TOXIN Snake toxins signature. GCg..CPpgddnlevk.CCtsP source prosite : PS00272 19) chain A residue 94-104 type prosite sequence EDCLYLNVWTP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP source prosite : PS00941 20) chain F residue 33 type SITE sequence M description Blocks the entrance of the active site gorge of hAChE => ECO:0000303|PubMed:23679855 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 22) chain A residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 23) chain A residue 265 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 350 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI4 25) chain A residue 464 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine source Swiss-Prot : SWS_FT_FI4

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