eF-site ID 6nea-A PDB Code 6nea Chain A click to enlarge Title Human Acetylcholinesterase in complex with reactivator, HLo7 Classification HYDROLASE Compound Acetylcholinesterase Source (ACES_HUMAN) Sequence A:  REDAELLVTVRGGRLRGIRLKTPGGPVSAFLGIPFAEPPM GPRRFLPPEPKQPWSGVVDATTFQSVCYQYVDTLYPGFEG TEMWNPNRELSEDCLYLNVWTPYPRPTSPTPVLVWIYGGG FYSGASSLDVYDGRFLVQAERTVLVSMNYRVGAFGFLALP GSREAPGNVGLLDQRLALQWVQENVAAFGGDPTSVTLFGE SAGAASVGMHLLSPPSRGLFHRAVLQSGAPNGPWATVGMG EARRRATQLAHLVGCPPGGNDTELVACLRTRPAQVLVNHE WHVLPQESVFRFSFVPVVDGDFLSDTPEALINAGDFHGLQ VLVGVVKDEGSYFLVYGAPGFSKDNESLISRAEFLAGVRV GVPQVSDLAAEAVVLHYTDWLHPEDPARLREALSDVVGDH NVVCPVAQLAGRLAAQGARVYAYVFEHRASTLSWPLWMGV PHGYEIEFIFGIPLDPSRNYTAEEKIFAQRLMRYWANFAR TGDPNEPAPQWPPYTAGAQQYVSLDLRPLEVRRGLRAQAC AFWNRFLPKLLSA Description Functional site 1) 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 2) chain A residue 86 type BINDING sequence W description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 3) chain A residue 133 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 337 type BINDING sequence Y description BINDING => ECO:0007744|PDB:4EY5 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 122 type BINDING sequence G description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 6) chain A residue 203 type BINDING sequence S description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 7) chain A residue 439 type BINDING sequence W description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 8) chain A residue 447 type BINDING sequence H description BINDING => ECO:0007744|PDB:4BDT source Swiss-Prot : SWS_FT_FI4 9) chain A residue 203 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 10) chain A residue 334 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2 11) chain A residue 447 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 12) chain A residue 190-205 type prosite sequence FGGDPTSVTLFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdptsVtLfGeSAG source prosite : PS00122 13) chain A residue 94-104 type prosite sequence EDCLYLNVWTP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNVWtP source prosite : PS00941 14) chain A residue 202 type BINDING sequence E description BINDING => ECO:0007744|PDB:4EY6 source Swiss-Prot : SWS_FT_FI5 15) 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 16) 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

Display surface Download Links