eF-site ID 6g5f-A PDB Code 6g5f Chain A 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 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 A residue 207 type sequence Q description binding site for residue GOL A 1302 source : AC2 5) chain A residue 275 type sequence Q description binding site for residue GOL A 1302 source : AC2 6) chain A residue 123 type sequence R description binding site for residue GOL A 1303 source : AC3 7) chain A residue 124 type sequence V description binding site for residue GOL A 1303 source : AC3 8) chain A residue 130 type sequence N description binding site for residue GOL A 1303 source : AC3 9) chain A residue 259 type sequence Q description binding site for residue MLI B 1301 source : AC4 10) chain A residue 374 type sequence F description binding site for residue MLI B 1301 source : AC4 11) chain A residue 376 type sequence D description binding site for residue MLI B 1301 source : AC4 12) chain A residue 230 type catalytic sequence H description 626 source MCSA : MCSA1 13) chain A residue 231 type catalytic sequence Q description 626 source MCSA : MCSA1 14) chain A residue 234 type catalytic sequence Y description 626 source MCSA : MCSA1 15) chain A residue 268 type catalytic sequence E description 626 source MCSA : MCSA1 16) chain A residue 370 type catalytic sequence R description 626 source MCSA : MCSA1 17) chain A residue 231 type ACT_SITE sequence Q description ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095 source Swiss-Prot : SWS_FT_FI1 18) 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 19) 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 20) 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

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