eF-site ID 5cci-E PDB Code 5cci Chain E 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 E:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLK KMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYN ESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGY NSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVK 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 E residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 12) chain E residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 13) chain E residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 14) chain E residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 15) chain E residue 303 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 16) chain E residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 17) chain E residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 18) chain E residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 19) chain E residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 20) chain E residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 21) chain E residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 22) chain E residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 23) chain E residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 24) chain E residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 25) chain E residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 26) chain E residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 27) chain E residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 28) chain E residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2

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