6KQI
Structure of an allosteric modulator bound to the CB1 cannabinoid receptor
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue 9GF A 1201 |
| Chain | Residue |
| A | SER173 |
| A | TRP356 |
| A | MET363 |
| A | PHE379 |
| A | SER383 |
| A | PHE174 |
| A | PHE177 |
| A | LYS192 |
| A | LEU193 |
| A | VAL196 |
| A | ILE267 |
| A | PHE268 |
| A | TYR275 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue 9GL A 1202 |
| Chain | Residue |
| A | HIS154 |
| A | GLY157 |
| A | SER158 |
| A | CYS238 |
| A | TRP241 |
| A | THR242 |
| A | ILE245 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue OLA A 1203 |
| Chain | Residue |
| A | LEU374 |
| A | VAL378 |
| A | PHE381 |
| A | CYS382 |
| A | LEU385 |
| A | OLC1207 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1204 |
| Chain | Residue |
| A | TRP255 |
| A | PHE278 |
| A | OLC1207 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 1205 |
| Chain | Residue |
| A | LEU124 |
| A | OLA1206 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1206 |
| Chain | Residue |
| A | LEU124 |
| A | THR125 |
| A | OLA1205 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | OLA1203 |
| A | OLA1204 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 1210 |
| Chain | Residue |
| A | PHE408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | LEU117-LEU142 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | HIS143-HIS154 | |
| A | ASP213-LYS232 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | PHE155-ILE175 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | ASP176-ASN187 | |
| A | ASN256-LYS273 | |
| A | ASP366-THR377 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | VAL188-ILE212 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | ALA233-TRP255 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | THR274-TRP299 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | LEU345-TYR365 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:27768894, ECO:0000269|PubMed:27851727 |
| Chain | Residue | Details |
| A | VAL378-LEU399 |
