eF-site ID 6g5f-ABP PDB Code 6g5f Chain A, B, P click to enlarge Title Crystal structure of an engineered Botulinum Neurotoxin type B mutant E1191M/S1199Y in complex with human synaptotagmin 1 Classification TOXIN Compound Botulinum neurotoxin type B Source (SYT1_HUMAN) Sequence A:  PVTINNFNYNDPIDNNNIIMMEPPFARGTGRYYKAFKITD RIWIIPERYTFGYKPEDFNKSSGIFNRDVCEYYDPDYLNT NDKKNIFLQTMIKLFNRIKSKPLGEKLLEMIINGIPYLGD RRVPLEEFNTNIASVTVNKLISNPGEVERKKGIFANLIIF GPGPVLNENETIDIGIQNHFASREGFGGIMQMKFCPEYVS VFNNVQENKGASIFNRRGYFSDPALILMHQLIYVLHGLYG IKVDDLPIVPNEKKFFMQSTDAIQAEELYTFGGQDPSIIT PSTDKSIYDKVLQNFRGIVDRLNKVLVCISDPNININIYK NKFKDKYKFVEDSEGKYSIDVESFDKLYKSLMFGFTETNI AENYKIKTRASYFSDSLPPVKIKNLLDNEIYTIEEGFNIS DKDMEKEYRGQNKAINKQAYEEISKEHLAVYKIQMCKSVK B:  APGICIDVDNEDLFFIADKNSFSDDLSKNERIEYNTQSNY IENDFPINELILDTDLISKIELPSENTESLTDFNVDVPVY EKQPAIKKIFTDENTIFQYLYSQTFPLDIRDISLTSSFDD ALLFSNKVYSFFSMDYIKTANKVVEAGLFAGWVKQIVNDF VIEANKSNTMDKIADISLIVPYIGLALNVGNETAKGNFEN AFEIAGASILLEFIPELLIPVVGAFLLESYIDNKNKIIKT IDNALTKRNEKWSDMYGLIVAQWLSTVNTQFYTIKEGMYK ALNYQAQALEEIIKYRYNIYSEKEKSNINIDFNDINSKLN EGINQAIDNINNFINGCSVSYLMKKMIPLAVEKLLDFDNT LKKNLLNYIDENKLYLIGSAEYEKSKVNKYLKTIMPFDLS IYTNDTILIEMFNKYNSEILNNIILNLRYKDNNLIDLSGY GAKVEVYDGVELNDKNQFKLTSSANSKIRVTQNQNIINSV FLDFSVSFWIRIPKYKNDGIQNYIHNEYTIINCMKNNSGW KISIRGNRIIWTLIDINGKTKSVFFEYNIREDISEYINRW FFVTITNNLNNAKIYINGKLESNTDIKDIREVIANGEIIF KLDGDIDRTQFIWMKYFSIFNTELSQSNIEERYKIQSYSE YLKDFWGNPLMYNKEYYMFNAGNKNSYIKLKKDSPVGEIL TRSKYNQNSKYINYRDLYIGEKFIIRRKSNSQSINDDIVR KEDYIYLDFFNLNQEWRVYTYKYFKKEEMKLFLAPIYDSD EFYNTIQIKEYDEQPTYSCQLLFKKDEESTDEIGLIGIHR FYESGIYKDYFCISKWYLKEVKRKPYNLKLGCNWQFIPKD EGWTE P:  KEDAFSKLKEKFMNELHK Description Functional site 1) chain A residue 69 type sequence D description binding site for residue GOL A 1301 source : AC1 2) chain A residue 259 type sequence Q description binding site for residue GOL A 1301 source : AC1 3) chain A residue 375 type sequence S description binding site for residue GOL A 1301 source : AC1 4) chain B residue 452 type sequence E description binding site for residue GOL A 1301 source : AC1 5) chain A residue 207 type sequence Q description binding site for residue GOL A 1302 source : AC2 6) chain A residue 275 type sequence Q description binding site for residue GOL A 1302 source : AC2 7) chain B residue 705 type sequence L description binding site for residue GOL A 1302 source : AC2 8) chain B residue 709 type sequence N description binding site for residue GOL A 1302 source : AC2 9) chain A residue 123 type sequence R description binding site for residue GOL A 1303 source : AC3 10) chain A residue 124 type sequence V description binding site for residue GOL A 1303 source : AC3 11) chain A residue 130 type sequence N description binding site for residue GOL A 1303 source : AC3 12) chain A residue 259 type sequence Q description binding site for residue MLI B 1301 source : AC4 13) chain A residue 374 type sequence F description binding site for residue MLI B 1301 source : AC4 14) chain A residue 376 type sequence D description binding site for residue MLI B 1301 source : AC4 15) chain B residue 452 type sequence E description binding site for residue MLI B 1301 source : AC4 16) chain B residue 454 type sequence L description binding site for residue MLI B 1301 source : AC4 17) chain B residue 456 type sequence F description binding site for residue MLI B 1301 source : AC4 18) chain B residue 710 type sequence T description binding site for residue MLI B 1301 source : AC4 19) chain B residue 713 type sequence Y description binding site for residue MLI B 1301 source : AC4 20) chain B residue 714 type sequence T description binding site for residue MLI B 1301 source : AC4 21) chain A residue 230 type catalytic sequence H description 626 source MCSA : MCSA1 22) chain A residue 231 type catalytic sequence Q description 626 source MCSA : MCSA1 23) chain A residue 234 type catalytic sequence Y description 626 source MCSA : MCSA1 24) chain A residue 268 type catalytic sequence E description 626 source MCSA : MCSA1 25) chain A residue 370 type catalytic sequence R description 626 source MCSA : MCSA1 26) chain A residue 231 type ACT_SITE sequence Q description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 268 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10932256, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 1189 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:4KBB source Swiss-Prot : SWS_FT_FI5 29) chain B residue 1240 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:14731268, ECO:0007744|PDB:4KBB source Swiss-Prot : SWS_FT_FI5 30) chain A residue 230 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:1429690, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 234 type BINDING sequence Y description BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10932256, ECO:0000305|PubMed:1429690, ECO:0007744|PDB:1EPW, ECO:0007744|PDB:1F31, ECO:0007744|PDB:2NP0 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 1025 type BINDING sequence N description BINDING => ECO:0007744|PDB:4KBB source Swiss-Prot : SWS_FT_FI4

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