3RK2
Truncated SNARE 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 1 |
| Chain | Residue |
| B | ASP231 |
| C | GLU52 |
| C | HOH92 |
| G | GLU13 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 4 |
| Chain | Residue |
| B | GLU228 |
| B | ASP231 |
| G | GLU10 |
| G | GLU13 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 2 |
| Chain | Residue |
| F | ASP231 |
| G | GLU52 |
| C | GLU13 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 84 |
| Chain | Residue |
| C | GLU13 |
| F | GLU228 |
| F | ASP231 |
Functional Information from PROSITE/UniProt
| site_id | PS00914 |
| Number of Residues | 40 |
| Details | SYNTAXIN Syntaxin / epimorphin family signature. RhseIikLEnsIrELhdMFmdMamlVesQGemIDrIEyn.V |
| Chain | Residue | Details |
| B | ARG198-VAL237 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)","evidences":[{"source":"PubMed","id":"19543288","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 124 |
| 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_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E)","evidences":[{"source":"PubMed","id":"9886085","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA)","evidences":[{"source":"PubMed","id":"9886085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15592454","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"(Microbial infection) Cleavage; by C.botulinum neurotoxin type C (BoNT/C)","evidences":[{"source":"PubMed","id":"9886085","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15592454","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60879","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
