eF-site ID 4qd2-ABCDEFGHIJ PDB Code 4qd2 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex Classification CELL ADHESION Compound Hemagglutinin component HA33 Source Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A) (CADH1_MOUSE) Sequence A:  ENIQEINTAISDNYTYNINNPFYILFTVNTTGIYKINAQN NLPSLKIYEAIGINYITGFDSPNAKSYLVVLLNKDKNYYI RVPQTSSNIENQIQFKREEGDLRNLMNSSVNIIDNLNSTG AHYYTRQSPDVHDYISYEFTIPGNFNNKDTSNIRLYTSYN QGIGTLFRVTETIDGYNLINIQQNLHLLNNTNSIRLLNGA IYILKVEVTELNNYNIRLHIDITN B:  ERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQ KWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSN RCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILS QPLLLLPNFDIYNSNQMFKLEKI C:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW NIRNPP D:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW NIRNPP E:  WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQ GADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAV SSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKN MFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGL STTAKAVITVKD F:  ENIQEINTAISDNYTYNINNNPFYILFTVNTTGIYKINAQ NNLPSLKIYEAIGINYITGFDSPNAKSYLVVLLNKDKNYY IRVPQTSSNIENQIQFKREEGDLRNLMNSSVNIIDNLNST GAHYYTRQSPDVHDYISYEFTIPGNFNNKDTSNIRLYTSY NQGIGTLFRVTETIDGYNLINIQQNLHLLNNTNSIRLLNG AIYILKVEVTELNNYNIRLHIDITN G:  ERTFLPNGNYNIKSIFSGSLYLNPVSKSLTFSNESSANNQ KWNVEYMAENRCFKISNVAEPNKYLSYDNFGFISLDSLSN RCYWFPIKIAVNTYIMLSLNKVNELDYAWDIYDTNENILS QPLLLLPNFDIYNSNQMFKLEKI H:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW NIRNPP I:  NSLNDKIVTISCKADTNLFFYQVAGNVSLFQQTRNYLERW RLIYDSNKAAYKIKSMDIHNTNLVLTWNAPTHNISTQQDS NADNQYWLLLKDIGNNSFIIASYKNPNLVLYADTVARNLK LSTLNNSNYIKFIIEDYIISDLNNFTCKISPILDLNKVVQ QVDVTNLNVNLYTWDYGRNQKWTIRYNEEKAAYQFFNTIL SNGVLTWIFSNGNTVRVSSSNDQNNDAQYWLINPVSDTDE TYTITNLRDTTKALDLYGGQTANGTAIQVFNYHGDDNQKW NIRNPP J:  WVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQ GADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAV SSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGA VPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKN MFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGL STTAKAVITVKD Description Functional site 1) chain E residue 11 type sequence E description BINDING SITE FOR RESIDUE CA E 301 source : AC1 2) chain E residue 67 type sequence D description BINDING SITE FOR RESIDUE CA E 301 source : AC1 3) chain E residue 69 type sequence E description BINDING SITE FOR RESIDUE CA E 301 source : AC1 4) chain E residue 103 type sequence D description BINDING SITE FOR RESIDUE CA E 301 source : AC1 5) chain E residue 11 type sequence E description BINDING SITE FOR RESIDUE CA E 302 source : AC2 6) chain E residue 69 type sequence E description BINDING SITE FOR RESIDUE CA E 302 source : AC2 7) chain E residue 100 type sequence D description BINDING SITE FOR RESIDUE CA E 302 source : AC2 8) chain E residue 101 type sequence Q description BINDING SITE FOR RESIDUE CA E 302 source : AC2 9) chain E residue 103 type sequence D description BINDING SITE FOR RESIDUE CA E 302 source : AC2 10) chain E residue 136 type sequence D description BINDING SITE FOR RESIDUE CA E 302 source : AC2 11) chain E residue 102 type sequence N description BINDING SITE FOR RESIDUE CA E 303 source : AC3 12) chain E residue 104 type sequence N description BINDING SITE FOR RESIDUE CA E 303 source : AC3 13) chain E residue 134 type sequence D description BINDING SITE FOR RESIDUE CA E 303 source : AC3 14) chain E residue 136 type sequence D description BINDING SITE FOR RESIDUE CA E 303 source : AC3 15) chain E residue 143 type sequence N description BINDING SITE FOR RESIDUE CA E 303 source : AC3 16) chain E residue 195 type sequence D description BINDING SITE FOR RESIDUE CA E 303 source : AC3 17) chain J residue 11 type sequence E description BINDING SITE FOR RESIDUE CA J 301 source : AC4 18) chain J residue 67 type sequence D description BINDING SITE FOR RESIDUE CA J 301 source : AC4 19) chain J residue 69 type sequence E description BINDING SITE FOR RESIDUE CA J 301 source : AC4 20) chain J residue 103 type sequence D description BINDING SITE FOR RESIDUE CA J 301 source : AC4 21) chain J residue 11 type sequence E description BINDING SITE FOR RESIDUE CA J 302 source : AC5 22) chain J residue 69 type sequence E description BINDING SITE FOR RESIDUE CA J 302 source : AC5 23) chain J residue 100 type sequence D description BINDING SITE FOR RESIDUE CA J 302 source : AC5 24) chain J residue 101 type sequence Q description BINDING SITE FOR RESIDUE CA J 302 source : AC5 25) chain J residue 103 type sequence D description BINDING SITE FOR RESIDUE CA J 302 source : AC5 26) chain J residue 104 type sequence N description BINDING SITE FOR RESIDUE CA J 302 source : AC5 27) chain J residue 136 type sequence D description BINDING SITE FOR RESIDUE CA J 302 source : AC5 28) chain J residue 102 type sequence N description BINDING SITE FOR RESIDUE CA J 303 source : AC6 29) chain J residue 104 type sequence N description BINDING SITE FOR RESIDUE CA J 303 source : AC6 30) chain J residue 134 type sequence D description BINDING SITE FOR RESIDUE CA J 303 source : AC6 31) chain J residue 136 type sequence D description BINDING SITE FOR RESIDUE CA J 303 source : AC6 32) chain J residue 143 type sequence N description BINDING SITE FOR RESIDUE CA J 303 source : AC6 33) chain J residue 195 type sequence D description BINDING SITE FOR RESIDUE CA J 303 source : AC6 34) chain E residue 96-106 type prosite sequence ITVTDQNDNRP description CADHERIN_1 Cadherin domain signature. ItVtDqNDNrP source prosite : PS00232 35) chain E residue 103 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 36) chain E residue 134 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 37) chain J residue 103 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 38) chain J residue 134 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 39) chain E residue 126 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI2 40) chain E residue 131 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI2 41) chain J residue 126 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI2 42) chain J residue 131 type CARBOHYD sequence S description O-linked (Man...) serine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI2 43) chain E residue 204 type CARBOHYD sequence T description O-linked (Man...) threonine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI3 44) chain J residue 204 type CARBOHYD sequence T description O-linked (Man...) threonine => ECO:0000269|PubMed:28973932 source Swiss-Prot : SWS_FT_FI3

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