eF-site ID 6o52-AB PDB Code 6o52 Chain A, B click to enlarge Title Room temperature structure of binary complex of native hAChE with BW284c51 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 86 type sequence W description binding site for residue EBW A 601 source : AC1 2) chain A residue 124 type sequence Y description binding site for residue EBW A 601 source : AC1 3) chain A residue 202 type sequence E description binding site for residue EBW A 601 source : AC1 4) chain A residue 203 type sequence S description binding site for residue EBW A 601 source : AC1 5) chain A residue 286 type sequence W description binding site for residue EBW A 601 source : AC1 6) chain A residue 297 type sequence F description binding site for residue EBW A 601 source : AC1 7) chain A residue 337 type sequence Y description binding site for residue EBW A 601 source : AC1 8) chain A residue 338 type sequence F description binding site for residue EBW A 601 source : AC1 9) chain A residue 341 type sequence Y description binding site for residue EBW A 601 source : AC1 10) chain A residue 447 type sequence H description binding site for residue EBW A 601 source : AC1 11) chain B residue 76 type sequence L description binding site for residue EBW B 601 source : AC2 12) chain B residue 86 type sequence W description binding site for residue EBW B 601 source : AC2 13) chain B residue 124 type sequence Y description binding site for residue EBW B 601 source : AC2 14) chain B residue 202 type sequence E description binding site for residue EBW B 601 source : AC2 15) chain B residue 203 type sequence S description binding site for residue EBW B 601 source : AC2 16) chain B residue 286 type sequence W description binding site for residue EBW B 601 source : AC2 17) chain B residue 297 type sequence F description binding site for residue EBW B 601 source : AC2 18) chain B residue 337 type sequence Y description binding site for residue EBW B 601 source : AC2 19) chain B residue 338 type sequence F description binding site for residue EBW B 601 source : AC2 20) chain B residue 341 type sequence Y description binding site for residue EBW B 601 source : AC2 21) chain B residue 447 type sequence H description binding site for residue EBW B 601 source : AC2 22) chain A residue 203 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 23) chain B residue 203 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 24) chain A residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 25) chain A residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 26) chain B residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 27) chain B residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 28) chain A residue 86 type BINDING sequence W description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 29) chain A residue 133 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 337 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 86 type BINDING sequence W description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 133 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 337 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 122 type BINDING sequence G description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 35) chain A residue 203 type BINDING sequence S description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 36) chain A residue 439 type BINDING sequence W description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 37) chain A residue 447 type BINDING sequence H description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 38) chain B residue 122 type BINDING sequence G description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 39) chain B residue 203 type BINDING sequence S description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 40) chain B residue 439 type BINDING sequence W description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 41) chain B residue 447 type BINDING sequence H description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 42) chain A residue 202 type BINDING sequence E description BINDING => ECO:0007744|PDB:4EY6 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 202 type BINDING sequence E description BINDING => ECO:0007744|PDB:4EY6 source Swiss-Prot : SWS_FT_FI5 44) 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 45) 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 46) 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 47) 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 48) 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 49) 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 50) chain A residue 190-205 type prosite sequence FGGDPTSVTLFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG source prosite : PS00122 51) 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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