1SFC
NEURONAL SYNAPTIC FUSION COMPLEX
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0016192 | biological_process | vesicle-mediated transport |
| B | 0005484 | molecular_function | SNAP receptor activity |
| B | 0006886 | biological_process | intracellular protein transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016192 | biological_process | vesicle-mediated transport |
| C | 0000149 | molecular_function | SNARE binding |
| C | 0005249 | molecular_function | voltage-gated potassium channel activity |
| C | 0017075 | molecular_function | syntaxin-1 binding |
| E | 0016020 | cellular_component | membrane |
| E | 0016192 | biological_process | vesicle-mediated transport |
| F | 0005484 | molecular_function | SNAP receptor activity |
| F | 0006886 | biological_process | intracellular protein transport |
| F | 0016020 | cellular_component | membrane |
| F | 0016192 | biological_process | vesicle-mediated transport |
| G | 0000149 | molecular_function | SNARE binding |
| G | 0005249 | molecular_function | voltage-gated potassium channel activity |
| G | 0017075 | molecular_function | syntaxin-1 binding |
| I | 0016020 | cellular_component | membrane |
| I | 0016192 | biological_process | vesicle-mediated transport |
| J | 0005484 | molecular_function | SNAP receptor activity |
| J | 0006886 | biological_process | intracellular protein transport |
| J | 0016020 | cellular_component | membrane |
| J | 0016192 | biological_process | vesicle-mediated transport |
| K | 0000149 | molecular_function | SNARE binding |
| K | 0005249 | molecular_function | voltage-gated potassium channel activity |
| K | 0017075 | molecular_function | syntaxin-1 binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SR D 288 |
| Chain | Residue |
| D | HOH516 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SR A 289 |
| Chain | Residue |
| A | ASP68 |
| A | HOH513 |
| I | SER75 |
| I | GLU78 |
| I | THR79 |
| I | HOH506 |
| I | HOH510 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SR A 290 |
| Chain | Residue |
| A | GLU78 |
| A | THR79 |
| A | HOH507 |
| I | ASP68 |
| I | MPD930 |
| A | SER75 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SR F 291 |
| Chain | Residue |
| F | ASP242 |
| F | GLU245 |
| F | HOH504 |
| F | HOH511 |
| J | ASP242 |
| J | GLU245 |
| J | HOH508 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SR J 292 |
| Chain | Residue |
| J | ASP218 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SR K 293 |
| Chain | Residue |
| G | ASP41 |
| K | GLU37 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SR B 294 |
| Chain | Residue |
| B | ASP218 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SR C 295 |
| Chain | Residue |
| C | GLU55 |
| C | HOH519 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SR C 296 |
| Chain | Residue |
| C | ASP51 |
| C | GLU55 |
| C | HOH519 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SR F 297 |
| Chain | Residue |
| F | ASP214 |
| F | ASP218 |
| F | HOH501 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SR G 298 |
| Chain | Residue |
| G | ASP51 |
| G | GLU55 |
| G | SR299 |
| G | SR300 |
| K | ASP51 |
| K | GLU55 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SR G 299 |
| Chain | Residue |
| G | ASP51 |
| G | SR298 |
| K | GLU52 |
| K | GLU55 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SR G 300 |
| Chain | Residue |
| G | GLU55 |
| G | SR298 |
| K | ASP51 |
| K | GLU55 |
| K | MPD929 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD F 926 |
| Chain | Residue |
| B | ASP231 |
| C | GLU52 |
| C | GLN53 |
| E | GLN71 |
| F | TYR235 |
| F | ASN236 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 927 |
| Chain | Residue |
| A | ARG86 |
| A | TRP89 |
| I | ASP57 |
| J | SER225 |
| J | MET229 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD A 928 |
| Chain | Residue |
| A | ASP65 |
| A | ASP68 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD K 929 |
| Chain | Residue |
| G | SR300 |
| K | LYS76 |
| K | ASP80 |
| L | GLU170 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD I 930 |
| Chain | Residue |
| A | GLN76 |
| A | THR79 |
| A | SR290 |
| I | ASP68 |
| I | ALA69 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MPD K 931 |
| Chain | Residue |
| K | GLN15 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD G 932 |
| Chain | Residue |
| F | GLU245 |
| G | HIS66 |
| G | GLN69 |
| G | ASP70 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 180 |
| Details | Domain: {"description":"v-SNARE coiled-coil homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU00290","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)","evidences":[{"source":"PubMed","id":"8505288","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)","evidences":[{"source":"PubMed","id":"8175689","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)","evidences":[{"source":"PubMed","id":"28770820","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.tetani tetanus toxin (tetX)","evidences":[{"source":"PubMed","id":"1331807","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG)","evidences":[{"source":"PubMed","id":"7910017","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 186 |
| Details | Domain: {"description":"t-SNARE coiled-coil homology","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)","evidences":[{"source":"PubMed","id":"7737992","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"12730201","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 12 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"UniProtKB","id":"Q16623","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 186 |
| Details | Domain: {"description":"t-SNARE coiled-coil homology 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 186 |
| Details | Domain: {"description":"t-SNARE coiled-coil homology 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00202","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 3 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)","evidences":[{"source":"PubMed","id":"8243676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8294407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8103915","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC and PKA","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60879","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"12459461","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






