eF-site ID 5cci-ABCDEF PDB Code 5cci Chain A, B, C, D, E, F click to enlarge Title Structure of the Mg2+-bound synaptotagmin-1 SNARE complex (short unit cell form) Classification ENDOCYTOSIS,EXOCYTOSIS Compound Vesicle-associated membrane protein 2 Source null (SYT1_RAT) Sequence A:  SNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRA DALQAGASQFETSAAKLKRKYW B:  MALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEM IDRIEYNVEHAVDYVERAVSDTKKAVK C:  ELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVM LDEQGEQLDRVEEGMNHINQDMKEAEKNLKDLG D:  MARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQID RIMEKADSNKTRIDEANQRATKML E:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLK KMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYN ESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGY NSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVK F:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKGDICFSLRYVPTAGKLTVVILEAKNLKKMSDPY VKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQ IQKVQVVVTVLDYDKGKNDAIGKVFVGYNSTGAELRHWSD MLANPRRPIAQWHTLQVEEEVDAMLAVK Description Functional site 1) chain E residue 303 type sequence D description binding site for residue MG E 501 source : AC1 2) chain E residue 309 type sequence D description binding site for residue MG E 501 source : AC1 3) chain E residue 363 type sequence D description binding site for residue MG E 501 source : AC1 4) chain E residue 364 type sequence Y description binding site for residue MG E 501 source : AC1 5) chain E residue 365 type sequence D description binding site for residue MG E 501 source : AC1 6) chain E residue 172 type sequence D description binding site for residue MG E 502 source : AC2 7) chain E residue 178 type sequence D description binding site for residue MG E 502 source : AC2 8) chain E residue 231 type sequence F description binding site for residue MG E 502 source : AC2 9) chain E residue 232 type sequence D description binding site for residue MG E 502 source : AC2 10) chain E residue 346 type sequence E description binding site for residue MG E 502 source : AC2 11) chain F residue 172 type sequence D description binding site for residue MG F 501 source : AC3 12) chain F residue 178 type sequence D description binding site for residue MG F 501 source : AC3 13) chain F residue 231 type sequence F description binding site for residue MG F 501 source : AC3 14) chain F residue 346 type sequence E description binding site for residue MG F 501 source : AC3 15) chain F residue 302 type sequence M description binding site for residue MG F 502 source : AC4 16) chain F residue 363 type sequence D description binding site for residue MG F 502 source : AC4 17) chain F residue 365 type sequence D description binding site for residue MG F 502 source : AC4 18) chain F residue 185 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 19) chain F residue 186 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 20) chain F residue 187 type sequence P description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 21) chain F residue 189 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 22) chain F residue 191 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 23) chain F residue 192 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 24) chain F residue 214 type sequence V description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 25) chain F residue 185 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 26) chain F residue 186 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 27) chain F residue 187 type sequence P description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 28) chain F residue 189 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 29) chain F residue 191 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 30) chain F residue 192 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 31) chain F residue 214 type sequence V description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 32) chain A residue 49-68 type prosite sequence NVDKVLERDQKLSELDDRAD description SYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD source prosite : PS00417 33) chain B residue 198-237 type prosite sequence RHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNV description SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V source prosite : PS00914 34) chain E residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 35) chain E residue 303 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 36) chain E residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 37) chain E residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 38) chain E residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 39) chain E residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 40) chain F residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 41) chain F residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 42) chain F residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 43) chain F residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 44) chain F residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 45) chain F residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 46) chain F residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 47) chain F residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 48) chain F residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 49) chain F residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 50) chain F residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 51) chain F residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 52) chain F residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 53) chain E residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 54) chain E residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 55) chain E residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 56) chain E residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 57) chain E residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 58) chain E residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 59) chain E residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 60) chain E residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 61) chain F residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 253 type MOD_RES sequence K description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 63) chain B residue 256 type MOD_RES sequence K description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 64) chain E residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 65) chain F residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 66) chain E residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 67) chain F residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 68) chain F residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 69) chain E residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 70) chain E residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 71) chain A residue 81 type SITE sequence A description (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269|PubMed:7910017 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links