1URQ
Crystal structure of neuronal Q-SNAREs in complex with R-SNARE motif of Tomosyn
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 |
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 | 1 |
Details | SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type E (BoNT/E) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 |
Chain | Residue | Details |
D | ARG179 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type A (BoNT/A, botA) => ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915 |
Chain | Residue | Details |
D | GLN196 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKC and PKA => ECO:0000269|PubMed:12459461 |
Chain | Residue | Details |
D | LYS200 | |
B | LYS253 | |
B | LYS256 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60879 |
Chain | Residue | Details |
D | SER153 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:12459461 |
Chain | Residue | Details |
D | SER186 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P60879 |
Chain | Residue | Details |
D | GLU147 | |
D | GLU150 | |
D | VAL152 | |
D | GLY154 |