eF-site ID 3ffz-AB PDB Code 3ffz Chain A, B click to enlarge Title Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation Classification HYDROLASE Compound Botulinum neurotoxin type E Source ORGANISM_SCIENTIFIC: Clostridium botulinum; Sequence A:  PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWI IPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKD RFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPD NQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETN SSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNCMNE FIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLI TNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKK IASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNI NKFNDIFKKLYSFTEFDLATKFQVKCRQTYIGQYKYFKLS NLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG RGLVKKIIRFCKNIVSVKGIRKSICIEINNGELFFVASEN SYNDDNINTPKEIDDTVTSNDLDQVILNFNSESAPGLSDE KLNLTIQNDAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQ KVPEGENNVNLTSSIDTALLEQPKIYTFFSSEFINNVNKP VQAALFVSWIQQVLVDFTTEANQKSTVDKIADISIVVPYI GLALNIGNEAQKGNFKDALELLGAGILLEFEPELLIPTIL VFTIKSFLGSSDNKNKVIKAINNALKERDEKWKEVYSFIV SNWMTKINTQFNKRKEQMYQALQNQVNAIKTIIESKYNSY TLEEKNELTNKYDIKQIENELNQKVSIAMNNIDRFLTESS ISYLMKIINEVKINKLREYDENVKTYLLNYIIQHGSILGE SQQELNSMVTDTLNNSIPFKLSSYTDDKILISYFNKFFKR IKSSSVLNMRYKNDKYVDTSGYDSNININGDVYKYPTNKN QFGIYNDKLSEVNISQNDYIIYDNKYKNFSISFWVRIPNY DNKIVNVNNEYTIINCMRDNNSGWKVSLNHNEIIWTLQDN AGINQKLAFNYGNANGISDYINKWIFVTITNDRLGDSKLY INGNLIDQKSILNLGNIHVSDNILFKIVNCSYTRYIGIRY FNIFDKELDETEIQTLYSNEPNTNILKDFWGNYLLYDKEY YLLNVLKPNNFIDRRKDSTLSINNIRSTILLANRLYSGIK VKIQRVNNSSTNDNLVRKNDQVYINFVASKTHLFPLYADT ATTNKEKTIKISSSGNRFNQVVVMNSVGNNCTMNFKNNNG NNIGLLGFKADTVVASTWYYTHMRDHTNSNGCFWNFISEE HGWQEK B:  PKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWI IPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKD RFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPD NQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETN SSNISLRNNYMPSNHGFGSIAIVTFSPEYSFRFNDNCMNE FIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLI TNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKK IASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNI NKFNDIFKKLYSFTEFDLATKFQVKCRQTYIGQYKYFKLS NLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITG RGLVKKIIRFCKNKSICIEINNGELFFVASENSYNDDNIN TPKEIDDTVTSNDLDQVILNFNSESAPGLSDEKLNLTIQN DAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQKVPEGENN VNLTSSIDTALLEQPKIYTFFSSEFINNVNKPVQAALFVS WIQQVLVDFTTEANQKSTVDKIADISIVVPYIGLALNIGN EAQKGNFKDALELLGAGILLEFEPELLIPTILVFTIKSFL GSSDNKNKVIKAINNALKERDEKWKEVYSFIVSNWMTKIN TQFNKRKEQMYQALQNQVNAIKTIIESKYNSYTLEEKNEL TNKYDIKQIENELNQKVSIAMNNIDRFLTESSISYLMKII NEVKINKLREYDENVKTYLLNYIIQHGSILGESQQELNSM VTDTLNNSIPFKLSSYTDDKILISYFNKFFKRIKSSSVLN MRYKNDKYVDTSGYDSNININGDVYKYPTNKNQFGIYNDK LSEVNISQNDYIIYDNKYKNFSISFWVRIPNYDNKIVNVN NEYTIINCMRDNNSGWKVSLNHNEIIWTLQDNAGINQKLA FNYGNANGISDYINKWIFVTITNDRLGDSKLYINGNLIDQ KSILNLGNIHVSDNILFKIVNCSYTRYIGIRYFNIFDKEL DETEIQTLYSNEPNTNILKDFWGNYLLYDKEYYLLNVLKP NNFIDRRKDSTLSINNIRSTILLANRLYSGIKVKIQRVNN SSTNDNLVRKNDQVYINFVASKTHLFPLYADTATTNKEKT IKISSSGNRFNQVVVMNSVGNNCTMNFKNNNGNNIGLLGF KADTVVASTWYYTHMRDHTNSNGCFWNFISEEHGWQEK Description Functional site 1) chain A residue 212 type sequence H description BINDING SITE FOR RESIDUE ZN A1300 source : AC1 2) chain A residue 216 type sequence H description BINDING SITE FOR RESIDUE ZN A1300 source : AC1 3) chain A residue 251 type sequence E description BINDING SITE FOR RESIDUE ZN A1300 source : AC1 4) chain A residue 544 type sequence A description BINDING SITE FOR RESIDUE NA A1301 source : AC2 5) chain A residue 547 type sequence E description BINDING SITE FOR RESIDUE NA A1301 source : AC2 6) chain A residue 548 type sequence Q description BINDING SITE FOR RESIDUE NA A1301 source : AC2 7) chain A residue 550 type sequence K description BINDING SITE FOR RESIDUE NA A1301 source : AC2 8) chain A residue 593 type sequence V description BINDING SITE FOR RESIDUE NA A1302 source : AC3 9) chain A residue 596 type sequence I description BINDING SITE FOR RESIDUE NA A1302 source : AC3 10) chain A residue 597 type sequence A description BINDING SITE FOR RESIDUE NA A1302 source : AC3 11) chain A residue 599 type sequence I description BINDING SITE FOR RESIDUE NA A1302 source : AC3 12) chain A residue 879 type sequence Y description BINDING SITE FOR RESIDUE ACT A1303 source : AC4 13) chain A residue 1041 type sequence Y description BINDING SITE FOR RESIDUE ACT A1303 source : AC4 14) chain B residue 212 type sequence H description BINDING SITE FOR RESIDUE ZN B1300 source : AC5 15) chain B residue 216 type sequence H description BINDING SITE FOR RESIDUE ZN B1300 source : AC5 16) chain B residue 251 type sequence E description BINDING SITE FOR RESIDUE ZN B1300 source : AC5 17) chain B residue 593 type sequence V description BINDING SITE FOR RESIDUE NA B1302 source : AC6 18) chain B residue 596 type sequence I description BINDING SITE FOR RESIDUE NA B1302 source : AC6 19) chain B residue 599 type sequence I description BINDING SITE FOR RESIDUE NA B1302 source : AC6 20) chain B residue 600 type sequence S description BINDING SITE FOR RESIDUE NA B1302 source : AC6 21) chain B residue 879 type sequence Y description BINDING SITE FOR RESIDUE ACT B1303 source : AC7 22) chain B residue 881 type sequence Y description BINDING SITE FOR RESIDUE ACT B1303 source : AC7 23) chain A residue 209-218 type prosite sequence TLMHELIHSL description ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLMHELIHSL source prosite : PS00142 24) chain A residue 213 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:15157097 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 213 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:15157097 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 212 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI2 27) chain A residue 216 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI2 28) chain B residue 212 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI2 29) chain B residue 216 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI2 30) chain A residue 251 type BINDING sequence E description BINDING => ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI3 31) chain B residue 251 type BINDING sequence E description BINDING => ECO:0007744|PDB:1T3A, ECO:0007744|PDB:1T3C, ECO:0007744|PDB:1ZKW, ECO:0007744|PDB:1ZKX, ECO:0007744|PDB:1ZL6, ECO:0007744|PDB:1ZN3, ECO:0007744|PDB:3FFZ source Swiss-Prot : SWS_FT_FI3

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