eF-site ID 2ack-A PDB Code 2ack Chain A click to enlarge Title ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA Classification HYDROLASE Compound ACETYLCHOLINESTERASE Source ORGANISM_COMMON: Pacific electric ray; ORGANISM_SCIENTIFIC: Torpedo californica; Sequence A:  SELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNM RFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEM WNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSG SSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQE APGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGG ASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRR RAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLP FDSIFRFSFVPVIDGEFFPTSLESMLNSGNFKKTQILLGV NKDEGSFFLLYGAPGFSKDSESKISREDFMSGVKLSVPHA NDLGLDAVTLQYTDWMDDNNGIKNRDGLDDIVGDHNVICP LMHFVNKYTKFGNGTYLYFFNHRASNLVWPEWMGVIHGYE IEFVFGLPLVKELNYTAEEEALSRRIMHYWATFAKTGNPN ESKWPLFTTKEQKFIDLNTEPMKVHQRLRVQMCVFWNQFL PKLLNAT Description Functional site 1) chain A residue 200 type sequence S description CATALYTIC TRIAD. source : CAT 2) chain A residue 440 type sequence H description CATALYTIC TRIAD. source : CAT 3) chain A residue 327 type sequence E description CATALYTIC TRIAD. source : CAT 4) chain A residue 84 type sequence W description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 5) chain A residue 119 type sequence G description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 6) chain A residue 121 type sequence Y description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 7) chain A residue 199 type sequence E description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 8) chain A residue 200 type sequence S description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 9) chain A residue 331 type sequence F description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 10) chain A residue 440 type sequence H description BINDING SITE FOR RESIDUE EDR A 999 source : AC1 11) chain A residue 416 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558, ECO:0000269|PubMed:1678899 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 457 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 13) chain A residue 533 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299 source Swiss-Prot : SWS_FT_FI5 14) chain A residue 59 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368299, ECO:0000269|PubMed:16763558 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 187-202 type prosite sequence FGGDPKTVTIFGESAG description CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpktVtIfGeSAG source prosite : PS00122 16) chain A residue 92-102 type prosite sequence EDCLYLNIWVP description CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYLNIWvP source prosite : PS00941 17) chain A residue 200 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI1 18) chain A residue 440 type ACT_SITE sequence H description Charge relay system source Swiss-Prot : SWS_FT_FI2 19) chain A residue 327 type ACT_SITE sequence E description Charge relay system source Swiss-Prot : SWS_FT_FI2

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