eF-site ID 5cci-F PDB Code 5cci Chain 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 Rattus norvegicus (Rat) (SYT1_RAT) Sequence F:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKGDICFSLRYVPTAGKLTVVILEAKNLKKMSDPY VKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQ IQKVQVVVTVLDYDKGKNDAIGKVFVGYNSTGAELRHWSD MLANPRRPIAQWHTLQVEEEVDAMLAVK Description Functional site 1) chain F residue 172 type sequence D description binding site for residue MG F 501 source : AC3 2) chain F residue 178 type sequence D description binding site for residue MG F 501 source : AC3 3) chain F residue 231 type sequence F description binding site for residue MG F 501 source : AC3 4) chain F residue 346 type sequence E description binding site for residue MG F 501 source : AC3 5) chain F residue 302 type sequence M description binding site for residue MG F 502 source : AC4 6) chain F residue 363 type sequence D description binding site for residue MG F 502 source : AC4 7) chain F residue 365 type sequence D description binding site for residue MG F 502 source : AC4 8) chain F residue 185 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 9) chain F residue 186 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 10) chain F residue 187 type sequence P description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 11) chain F residue 189 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 12) chain F residue 191 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 13) chain F residue 192 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 14) chain F residue 214 type sequence V description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC5 15) chain F residue 185 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 16) chain F residue 186 type sequence L description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 17) chain F residue 187 type sequence P description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 18) chain F residue 189 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 19) chain F residue 191 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 20) chain F residue 192 type sequence K description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 21) chain F residue 214 type sequence V description binding site for Di-peptide ASP F 188 and LYS F 190 source : AC6 22) chain F residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 23) chain F residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 24) chain F residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 25) chain F residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 26) chain F residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 29) chain F residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 30) chain F residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 31) chain F residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 32) chain F residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 33) chain F residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 34) chain F residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 35) chain F residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 36) chain F residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 37) chain F residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 38) chain F residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2

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