eF-site ID 2c9t-ABCDEFGHIJKMOPQRST PDB Code 2c9t Chain A, B, C, D, E, F, G, H, I, J, K, M, O, P, Q, R, S, T click to enlarge Title Crystal Structure Of Acetylcholine Binding Protein (AChBP) From Aplysia Californica In Complex With alpha-Conotoxin ImI Classification RECEPTOR/TOXIN Compound SOLUBLE ACETYLCHOLINE RECEPTOR Source ORGANISM_COMMON: CALIFORNIA SEA HARE; ORGANISM_SCIENTIFIC: APLYSIA CALIFORNICA; Sequence A:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER B:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER C:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER D:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER E:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER F:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER G:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER H:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER I:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER J:  QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVK VDSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRTSA ADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQ VDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVV KFRER K:  GCCSDPRCAWRCX M:  GCCSDPRCAWRCX O:  GCCSDPRCAWRCX P:  GCCSDPRCAWRCX Q:  GCCSDPRCAWRCX R:  GCCSDPRCAWRCX S:  GCCSDPRCAWRCX T:  GCCSDPRCAWRCX Description Functional site 1) chain K residue 10 type sequence W description BINDING SITE FOR RESIDUE NH2 K 13 source : AC1 2) chain K residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 K 13 source : AC1 3) chain K residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 K 13 source : AC1 4) chain M residue 9 type sequence A description BINDING SITE FOR RESIDUE NH2 M 13 source : AC2 5) chain M residue 10 type sequence W description BINDING SITE FOR RESIDUE NH2 M 13 source : AC2 6) chain M residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 M 13 source : AC2 7) chain M residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 M 13 source : AC2 8) chain O residue 9 type sequence A description BINDING SITE FOR RESIDUE NH2 O 13 source : AC3 9) chain O residue 10 type sequence W description BINDING SITE FOR RESIDUE NH2 O 13 source : AC3 10) chain O residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 O 13 source : AC3 11) chain O residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 O 13 source : AC3 12) chain P residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 P 13 source : AC4 13) chain P residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 P 13 source : AC4 14) chain Q residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 Q 13 source : AC5 15) chain Q residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 Q 13 source : AC5 16) chain R residue 10 type sequence W description BINDING SITE FOR RESIDUE NH2 R 13 source : AC6 17) chain R residue 11 type sequence R description BINDING SITE FOR RESIDUE NH2 R 13 source : AC6 18) chain R residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 R 13 source : AC6 19) chain J residue 57 type sequence R description BINDING SITE FOR RESIDUE NH2 S 13 source : AC7 20) chain S residue 9 type sequence A description BINDING SITE FOR RESIDUE NH2 S 13 source : AC7 21) chain S residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 S 13 source : AC7 22) chain F residue 57 type sequence R description BINDING SITE FOR RESIDUE NH2 T 13 source : AC8 23) chain T residue 9 type sequence A description BINDING SITE FOR RESIDUE NH2 T 13 source : AC8 24) chain T residue 12 type sequence C description BINDING SITE FOR RESIDUE NH2 T 13 source : AC8 25) chain K residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 26) chain M residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 27) chain O residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 28) chain O residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 29) chain O residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 30) chain O residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 31) chain O residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 32) chain P residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 33) chain P residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 34) chain P residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 35) chain P residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 36) chain K residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 37) chain P residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 38) chain Q residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 39) chain Q residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 40) chain Q residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 41) chain Q residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 42) chain Q residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 43) chain R residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 44) chain R residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 45) chain R residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 46) chain R residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 47) chain K residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 48) chain R residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 49) chain S residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 50) chain S residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 51) chain S residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 52) chain S residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 53) chain S residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 54) chain T residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 55) chain T residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 56) chain T residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 57) chain T residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 58) chain K residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 59) chain T residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 60) chain K residue 10 type SITE sequence W description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 61) chain M residue 5 type SITE sequence D description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 62) chain M residue 6 type SITE sequence P description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 63) chain M residue 7 type SITE sequence R description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 64) chain M residue 9 type SITE sequence A description Important for binding to human alpha-7 nAChR => ECO:0000305|PubMed:15609996 source Swiss-Prot : SWS_FT_FI1 65) chain K residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 66) chain M residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 67) chain O residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 68) chain P residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 69) chain Q residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 70) chain R residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 71) chain S residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 72) chain T residue 12 type MOD_RES sequence C description Cysteine amide => ECO:0000269|PubMed:8206995 source Swiss-Prot : SWS_FT_FI2 73) chain K residue 2-12 type prosite sequence CCSDPRCAWRC description ALPHA_CONOTOXIN Alpha-conotoxin family signature. CCSdPRCA....WRC source prosite : PS60014

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