eF-site ID 5kj8-F PDB Code 5kj8 Chain F click to enlarge Title Structure of the Ca2+-bound synaptotagmin-1 SNARE complex (long unit cell form) - from synchrotron diffraction Classification ENDOCYTOSIS,EXOCYTOSIS Compound Vesicle-associated membrane protein 3 Source Rattus norvegicus (Rat) (SYT1_RAT) Sequence F:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKEEQLGDICFSLRYVPTAGKLTVVILEAKNLKKM DGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFS FEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTG AELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAV Description Functional site 1) chain F residue 172 type sequence D description binding site for residue CA F 501 source : AC6 2) chain F residue 178 type sequence D description binding site for residue CA F 501 source : AC6 3) chain F residue 230 type sequence D description binding site for residue CA F 501 source : AC6 4) chain F residue 231 type sequence F description binding site for residue CA F 501 source : AC6 5) chain F residue 172 type sequence D description binding site for residue CA F 502 source : AC7 6) chain F residue 230 type sequence D description binding site for residue CA F 502 source : AC7 7) chain F residue 232 type sequence D description binding site for residue CA F 502 source : AC7 8) chain F residue 324 type sequence K description binding site for residue CA F 502 source : AC7 9) chain F residue 303 type sequence D description binding site for residue CA F 503 source : AC8 10) chain F residue 309 type sequence D description binding site for residue CA F 503 source : AC8 11) chain F residue 363 type sequence D description binding site for residue CA F 503 source : AC8 12) chain F residue 364 type sequence Y description binding site for residue CA F 503 source : AC8 13) chain F residue 172 type sequence D description binding site for residue CA F 504 source : AC9 14) chain F residue 176 type sequence T description binding site for residue CA F 504 source : AC9 15) chain F residue 177 type sequence S description binding site for residue CA F 504 source : AC9 16) chain F residue 178 type sequence D description binding site for residue CA F 504 source : AC9 17) chain F residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 18) chain F residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 19) chain F residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 20) chain F residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 21) chain F residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 24) chain F residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 25) chain F residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 26) chain F residue 303 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 29) chain F residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 30) chain F residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 31) chain F residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 32) chain F residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 33) chain F residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 34) chain F residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4

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