eF-site ID 1sfc-ABCDEFGHIJKL PDB Code 1sfc Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title NEURONAL SYNAPTIC FUSION COMPLEX Classification TRANSPORT PROTEIN Compound PROTEIN (SYNAPTOBREVIN 2) Source null (SNP25_RAT) Sequence A:  NLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELD DRADALQAGASQFETSAAKLKRKYWWKNL B:  SKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQG EMIDRIEYNVEHAVDYVERAVSDTKKAVKYQS C:  MRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRT LVMLDEQGEQLDRVEEGMNHINQDMKEAEKNLKDLGK D:  GGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNE IDTQNRQIDRIMEKADSNKTRIDEANQRATKMLG E:  SNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRA DALQAGASQFETSAAKLKRKYWWKNLKMM F:  KQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGE MIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKA G:  EEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLD EQGEQLDRVEEGMNHINQDMKEAEKNLKDLGK H:  GFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEI DTQNRQIDRIMEKADSNKTRIDEANQRATKML I:  LTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDD RADALQAGASQFETSAAKLKRKYWWKNLK J:  SISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVES QGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQS K:  LEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVML DEQGEQLDRVEEGMNHINQDMKEAEKNLKDLGK L:  GFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEI DTQNRQIDRIMEKADSNKTRIDEANQRATKMLG Description Functional site 1) chain A residue 68 type sequence D description BINDING SITE FOR RESIDUE SR A 289 source : AC2 2) chain I residue 75 type sequence S description BINDING SITE FOR RESIDUE SR A 289 source : AC2 3) chain I residue 78 type sequence E description BINDING SITE FOR RESIDUE SR A 289 source : AC2 4) chain I residue 79 type sequence T description BINDING SITE FOR RESIDUE SR A 289 source : AC2 5) chain A residue 75 type sequence S description BINDING SITE FOR RESIDUE SR A 290 source : AC3 6) chain A residue 78 type sequence E description BINDING SITE FOR RESIDUE SR A 290 source : AC3 7) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE SR A 290 source : AC3 8) chain I residue 68 type sequence D description BINDING SITE FOR RESIDUE SR A 290 source : AC3 9) chain F residue 242 type sequence D description BINDING SITE FOR RESIDUE SR F 291 source : AC4 10) chain F residue 245 type sequence E description BINDING SITE FOR RESIDUE SR F 291 source : AC4 11) chain J residue 242 type sequence D description BINDING SITE FOR RESIDUE SR F 291 source : AC4 12) chain J residue 245 type sequence E description BINDING SITE FOR RESIDUE SR F 291 source : AC4 13) chain J residue 218 type sequence D description BINDING SITE FOR RESIDUE SR J 292 source : AC5 14) chain G residue 41 type sequence D description BINDING SITE FOR RESIDUE SR K 293 source : AC6 15) chain K residue 37 type sequence E description BINDING SITE FOR RESIDUE SR K 293 source : AC6 16) chain B residue 218 type sequence D description BINDING SITE FOR RESIDUE SR B 294 source : AC7 17) chain C residue 55 type sequence E description BINDING SITE FOR RESIDUE SR C 295 source : AC8 18) chain C residue 51 type sequence D description BINDING SITE FOR RESIDUE SR C 296 source : AC9 19) chain C residue 55 type sequence E description BINDING SITE FOR RESIDUE SR C 296 source : AC9 20) chain F residue 214 type sequence D description BINDING SITE FOR RESIDUE SR F 297 source : BC1 21) chain F residue 218 type sequence D description BINDING SITE FOR RESIDUE SR F 297 source : BC1 22) chain G residue 51 type sequence D description BINDING SITE FOR RESIDUE SR G 298 source : BC2 23) chain G residue 55 type sequence E description BINDING SITE FOR RESIDUE SR G 298 source : BC2 24) chain K residue 51 type sequence D description BINDING SITE FOR RESIDUE SR G 298 source : BC2 25) chain K residue 55 type sequence E description BINDING SITE FOR RESIDUE SR G 298 source : BC2 26) chain G residue 51 type sequence D description BINDING SITE FOR RESIDUE SR G 299 source : BC3 27) chain K residue 52 type sequence E description BINDING SITE FOR RESIDUE SR G 299 source : BC3 28) chain K residue 55 type sequence E description BINDING SITE FOR RESIDUE SR G 299 source : BC3 29) chain G residue 55 type sequence E description BINDING SITE FOR RESIDUE SR G 300 source : BC4 30) chain K residue 51 type sequence D description BINDING SITE FOR RESIDUE SR G 300 source : BC4 31) chain K residue 55 type sequence E description BINDING SITE FOR RESIDUE SR G 300 source : BC4 32) chain B residue 231 type sequence D description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 33) chain C residue 52 type sequence E description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 34) chain C residue 53 type sequence Q description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 35) chain E residue 71 type sequence Q description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 36) chain F residue 235 type sequence Y description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 37) chain F residue 236 type sequence N description BINDING SITE FOR RESIDUE MPD F 926 source : BC5 38) chain A residue 86 type sequence R description BINDING SITE FOR RESIDUE MPD A 927 source : BC6 39) chain A residue 89 type sequence W description BINDING SITE FOR RESIDUE MPD A 927 source : BC6 40) chain I residue 57 type sequence D description BINDING SITE FOR RESIDUE MPD A 927 source : BC6 41) chain J residue 225 type sequence S description BINDING SITE FOR RESIDUE MPD A 927 source : BC6 42) chain J residue 229 type sequence M description BINDING SITE FOR RESIDUE MPD A 927 source : BC6 43) chain A residue 65 type sequence D description BINDING SITE FOR RESIDUE MPD A 928 source : BC7 44) chain A residue 68 type sequence D description BINDING SITE FOR RESIDUE MPD A 928 source : BC7 45) chain K residue 76 type sequence K description BINDING SITE FOR RESIDUE MPD K 929 source : BC8 46) chain K residue 80 type sequence D description BINDING SITE FOR RESIDUE MPD K 929 source : BC8 47) chain L residue 170 type sequence E description BINDING SITE FOR RESIDUE MPD K 929 source : BC8 48) chain A residue 76 type sequence Q description BINDING SITE FOR RESIDUE MPD I 930 source : BC9 49) chain A residue 79 type sequence T description BINDING SITE FOR RESIDUE MPD I 930 source : BC9 50) chain I residue 68 type sequence D description BINDING SITE FOR RESIDUE MPD I 930 source : BC9 51) chain I residue 69 type sequence A description BINDING SITE FOR RESIDUE MPD I 930 source : BC9 52) chain K residue 15 type sequence Q description BINDING SITE FOR RESIDUE MPD K 931 source : CC1 53) chain F residue 245 type sequence E description BINDING SITE FOR RESIDUE MPD G 932 source : CC2 54) chain G residue 66 type sequence H description BINDING SITE FOR RESIDUE MPD G 932 source : CC2 55) chain G residue 69 type sequence Q description BINDING SITE FOR RESIDUE MPD G 932 source : CC2 56) chain G residue 70 type sequence D description BINDING SITE FOR RESIDUE MPD G 932 source : CC2 57) chain H residue 180 type SITE sequence R description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI1 58) chain L residue 180 type SITE sequence R description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI1 59) chain D residue 180 type SITE sequence R description (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI1 60) chain H residue 197 type SITE sequence Q description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI2 61) chain L residue 197 type SITE sequence Q description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI2 62) chain D residue 197 type SITE sequence Q description (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 source Swiss-Prot : SWS_FT_FI2 63) chain J residue 253 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 64) chain J residue 256 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 65) chain B residue 256 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 66) chain F residue 252 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 67) chain F residue 253 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 68) chain F residue 256 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 69) chain J residue 252 type MOD_RES sequence K description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 70) chain H residue 138 type MOD_RES sequence T description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 71) chain L residue 138 type MOD_RES sequence T description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 138 type MOD_RES sequence T description Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI3 73) chain H residue 154 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P60879 source Swiss-Prot : SWS_FT_FI4 74) chain L residue 154 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P60879 source Swiss-Prot : SWS_FT_FI4 75) chain D residue 154 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P60879 source Swiss-Prot : SWS_FT_FI4 76) chain H residue 187 type MOD_RES sequence S description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI5 77) chain L residue 187 type MOD_RES sequence S description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI5 78) chain D residue 187 type MOD_RES sequence S description Phosphoserine; by PKC => ECO:0000269|PubMed:12459461 source Swiss-Prot : SWS_FT_FI5 79) chain E 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_FI6 80) chain I 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_FI6 81) 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_FI6 82) chain B residue 198-237 type prosite sequence RHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNV description SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V source prosite : PS00914 83) chain A residue 49-68 type prosite sequence NVDKVLERDQKLSELDDRAD description SYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD source prosite : PS00417

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