eF-site ID 6o4w-AB PDB Code 6o4w Chain A, B click to enlarge Title Binary complex of native hAChE with Donepezil Classification HYDROLASE Compound Acetylcholinesterase Source (ACES_HUMAN) Sequence A:  EDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMG PRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGT EMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGF YSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPG SREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGES AGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGE ARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVN HEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHG LQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGV RVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVG DHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWM GVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANF ARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRG LRAQACAFWNRFLPKLLSAT B:  EDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPMG PRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEGT EMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGGF YSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALPG SREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGES AGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMGE ARRRATQLAHLVGCPPGGTGGNDTELVACLRTRPAQVLVN HEWHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHG LQVLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGV RVGVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVG DHNVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWM GVPHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANF ARTGDPNEPRDPKAPQWPPYTAGAQQYVSLDLRPLEVRRG LRAQACAFWNRFLPKLLSAT Description Functional site 1) chain A residue 81 type sequence E description binding site for residue GOL A 601 source : AC1 2) chain A residue 85 type sequence M description binding site for residue GOL A 601 source : AC1 3) chain A residue 436 type sequence T description binding site for residue GOL A 601 source : AC1 4) chain A residue 437 type sequence L description binding site for residue GOL A 601 source : AC1 5) chain A residue 438 type sequence S description binding site for residue GOL A 601 source : AC1 6) chain A residue 449 type sequence Y description binding site for residue GOL A 601 source : AC1 7) chain A residue 452 type sequence E description binding site for residue GOL A 601 source : AC1 8) chain A residue 341 type sequence Y description binding site for residue GOL A 602 source : AC2 9) chain A residue 46 type sequence R description binding site for residue GOL A 603 source : AC3 10) chain A residue 274 type sequence R description binding site for residue GOL A 603 source : AC3 11) chain A residue 275 type sequence T description binding site for residue GOL A 603 source : AC3 12) chain A residue 277 type sequence P description binding site for residue GOL A 603 source : AC3 13) chain A residue 72 type sequence Y description binding site for residue E20 A 604 source : AC4 14) chain A residue 86 type sequence W description binding site for residue E20 A 604 source : AC4 15) chain A residue 124 type sequence Y description binding site for residue E20 A 604 source : AC4 16) chain A residue 202 type sequence E description binding site for residue E20 A 604 source : AC4 17) chain A residue 286 type sequence W description binding site for residue E20 A 604 source : AC4 18) chain A residue 293 type sequence S description binding site for residue E20 A 604 source : AC4 19) chain A residue 295 type sequence F description binding site for residue E20 A 604 source : AC4 20) chain A residue 337 type sequence Y description binding site for residue E20 A 604 source : AC4 21) chain A residue 338 type sequence F description binding site for residue E20 A 604 source : AC4 22) chain A residue 341 type sequence Y description binding site for residue E20 A 604 source : AC4 23) chain A residue 333 type sequence D description binding site for residue NO3 A 605 source : AC5 24) chain A residue 442 type sequence W description binding site for residue NO3 A 605 source : AC5 25) chain B residue 81 type sequence E description binding site for residue GOL B 601 source : AC6 26) chain B residue 85 type sequence M description binding site for residue GOL B 601 source : AC6 27) chain B residue 436 type sequence T description binding site for residue GOL B 601 source : AC6 28) chain B residue 437 type sequence L description binding site for residue GOL B 601 source : AC6 29) chain B residue 438 type sequence S description binding site for residue GOL B 601 source : AC6 30) chain B residue 449 type sequence Y description binding site for residue GOL B 601 source : AC6 31) chain B residue 452 type sequence E description binding site for residue GOL B 601 source : AC6 32) chain B residue 76 type sequence L description binding site for residue GOL B 602 source : AC7 33) chain B residue 341 type sequence Y description binding site for residue GOL B 602 source : AC7 34) chain B residue 274 type sequence R description binding site for residue GOL B 603 source : AC8 35) chain B residue 277 type sequence P description binding site for residue GOL B 603 source : AC8 36) chain B residue 72 type sequence Y description binding site for residue E20 B 604 source : AC9 37) chain B residue 86 type sequence W description binding site for residue E20 B 604 source : AC9 38) chain B residue 124 type sequence Y description binding site for residue E20 B 604 source : AC9 39) chain B residue 202 type sequence E description binding site for residue E20 B 604 source : AC9 40) chain B residue 286 type sequence W description binding site for residue E20 B 604 source : AC9 41) chain B residue 293 type sequence S description binding site for residue E20 B 604 source : AC9 42) chain B residue 295 type sequence F description binding site for residue E20 B 604 source : AC9 43) chain B residue 337 type sequence Y description binding site for residue E20 B 604 source : AC9 44) chain B residue 338 type sequence F description binding site for residue E20 B 604 source : AC9 45) chain B residue 341 type sequence Y description binding site for residue E20 B 604 source : AC9 46) chain B residue 332 type sequence K description binding site for residue NO3 B 605 source : AD1 47) chain B residue 333 type sequence D description binding site for residue NO3 B 605 source : AD1 48) chain B residue 396 type sequence E description binding site for residue NO3 B 605 source : AD1 49) chain B residue 442 type sequence W description binding site for residue NO3 B 605 source : AD1 50) chain B residue 36 type sequence P description binding site for residue NO3 B 606 source : AD2 51) chain B residue 98 type sequence Y description binding site for residue NO3 B 606 source : AD2 52) chain B residue 88 type sequence P description binding site for residue NO3 B 607 source : AD3 53) chain B residue 89 type sequence N description binding site for residue NO3 B 607 source : AD3 54) chain B residue 90 type sequence R description binding site for residue NO3 B 607 source : AD3 55) chain B residue 91 type sequence E description binding site for residue NO3 B 607 source : AD3 56) chain A residue 190-205 type prosite sequence FGGDPTSVTLFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG source prosite : PS00122 57) chain A residue 203 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 58) chain B residue 203 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 59) chain A residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 60) chain A residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 61) chain B residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 62) chain B residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 63) chain A residue 86 type BINDING sequence W description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 64) chain A residue 133 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 337 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 66) chain B residue 86 type BINDING sequence W description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 133 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 68) chain B residue 337 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 69) chain A residue 122 type BINDING sequence G description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 70) chain A residue 439 type BINDING sequence W description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 71) chain A residue 447 type BINDING sequence H description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 72) chain B residue 122 type BINDING sequence G description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 73) chain B residue 203 type BINDING sequence S description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 74) chain B residue 439 type BINDING sequence W description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 75) chain B residue 447 type BINDING sequence H description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 76) chain A residue 203 type BINDING sequence S description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 77) chain A residue 202 type BINDING sequence E description BINDING => ECO:0007744|PDB:4EY6 source Swiss-Prot : SWS_FT_FI5 78) chain B residue 202 type BINDING sequence E description BINDING => ECO:0007744|PDB:4EY6 source Swiss-Prot : SWS_FT_FI5 79) chain A residue 265 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7 source Swiss-Prot : SWS_FT_FI6 80) chain B residue 265 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7 source Swiss-Prot : SWS_FT_FI6 81) chain A residue 350 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:20408548, ECO:0000269|PubMed:23035744, ECO:0000269|PubMed:23679855, ECO:0007744|PDB:1B41, ECO:0007744|PDB:1F8U, ECO:0007744|PDB:2X8B, ECO:0007744|PDB:4BDT, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7, ECO:0007744|PDB:4EY8 source Swiss-Prot : SWS_FT_FI7 82) chain B residue 350 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11053835, ECO:0000269|PubMed:20408548, ECO:0000269|PubMed:23035744, ECO:0000269|PubMed:23679855, ECO:0007744|PDB:1B41, ECO:0007744|PDB:1F8U, ECO:0007744|PDB:2X8B, ECO:0007744|PDB:4BDT, ECO:0007744|PDB:4EY4, ECO:0007744|PDB:4EY5, ECO:0007744|PDB:4EY6, ECO:0007744|PDB:4EY7, ECO:0007744|PDB:4EY8 source Swiss-Prot : SWS_FT_FI7 83) chain A residue 464 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY8 source Swiss-Prot : SWS_FT_FI8 84) chain B residue 464 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23035744, ECO:0007744|PDB:4EY8 source Swiss-Prot : SWS_FT_FI8 85) chain A residue 94-104 type prosite sequence EDCLYLNVWTP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP source prosite : PS00941

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