eF-site ID 5kj8-K PDB Code 5kj8 Chain K 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 K:  KLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPY VKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELG GKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWR DLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLK KMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYN ESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGY NSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAV Description Functional site 1) chain K residue 302 type sequence M description binding site for residue CA K 501 source : AD1 2) chain K residue 303 type sequence D description binding site for residue CA K 501 source : AD1 3) chain K residue 307 type sequence L description binding site for residue CA K 501 source : AD1 4) chain K residue 308 type sequence S description binding site for residue CA K 501 source : AD1 5) chain K residue 363 type sequence D description binding site for residue CA K 501 source : AD1 6) chain K residue 303 type sequence D description binding site for residue CA K 502 source : AD2 7) chain K residue 309 type sequence D description binding site for residue CA K 502 source : AD2 8) chain K residue 363 type sequence D description binding site for residue CA K 502 source : AD2 9) chain K residue 364 type sequence Y description binding site for residue CA K 502 source : AD2 10) chain K residue 365 type sequence D description binding site for residue CA K 502 source : AD2 11) chain K residue 172 type sequence D description binding site for residue CA K 503 source : AD3 12) chain K residue 230 type sequence D description binding site for residue CA K 503 source : AD3 13) chain K residue 231 type sequence F description binding site for residue CA K 503 source : AD3 14) chain K residue 232 type sequence D description binding site for residue CA K 503 source : AD3 15) chain K residue 172 type sequence D description binding site for residue CA K 504 source : AD4 16) chain K residue 178 type sequence D description binding site for residue CA K 504 source : AD4 17) chain K residue 231 type sequence F description binding site for residue CA K 504 source : AD4 18) chain K residue 171 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 19) chain K residue 172 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 20) chain K residue 178 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 21) chain K residue 230 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 22) chain K residue 231 type BINDING sequence F description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 23) chain K residue 232 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 24) chain K residue 235 type BINDING sequence S description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 25) chain K residue 236 type BINDING sequence K description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 26) chain K residue 238 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 27) chain K residue 303 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 28) chain K residue 309 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 29) chain K residue 363 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 30) chain K residue 365 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 31) chain K residue 371 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00041 source Swiss-Prot : SWS_FT_FI1 32) chain K residue 229 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI2 33) chain K residue 264 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P46096 source Swiss-Prot : SWS_FT_FI3 34) chain K residue 342 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4 35) chain K residue 344 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI4

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