eF-site ID 6hy7-AB PDB Code 6hy7 Chain A, B click to enlarge Title Crystal structure of alpha9 nAChR extracellular domain in complex with alpha-conotoxin RgIA Classification TOXIN Compound Neuronal acetylcholine receptor subunit alpha-9 Source (CA1A_CONRE) Sequence A:  DGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQ IKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSIR IPSDLVWRPDIVLYNKADDEEPVNTNVVLRYDGLITWDAP AITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDIFNA LDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVT FTLLLKRRSH B:  GCCSDPRCRYRCX Description Functional site 1) chain B residue 5 type SITE sequence D description Key residue for potent inhibition of the rat CHRNA9-CHRNA10 nAChR => ECO:0000269|PubMed:18295795 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 6 type SITE sequence P description Key residue for potent inhibition of the rat CHRNA9-CHRNA10 nAChR => ECO:0000269|PubMed:18295795 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 7 type SITE sequence R description Key residue for potent inhibition of the rat CHRNA9-CHRNA10 nAChR => ECO:0000269|PubMed:18295795 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 9 type SITE sequence R description Key residue for potent inhibition of the rat CHRNA9-CHRNA10 nAChR => ECO:0000269|PubMed:18295795 source Swiss-Prot : SWS_FT_FI1 5) chain B residue 11 type SITE sequence R description Binds to the Glu-221 of the rat nAChR CHRNA10 subunit => ECO:0000305|PubMed:25740413 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 130-144 type prosite sequence CVVDVTYFPFDNQQC description NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CvVdVtyFPfDnqqC source prosite : PS00236 7) chain B residue 2-12 type prosite sequence CCSDPRCRYRC description ALPHA_CONOTOXIN Alpha-conotoxin family signature. CCSdPRCR....YRC source prosite : PS60014 8) chain A residue 32 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 145 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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