6RV3
Crystal structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1) in a closed conformation with a bound inhibitor BAY 1000493
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005252 | molecular_function | open rectifier potassium channel activity |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| B | 0005252 | molecular_function | open rectifier potassium channel activity |
| B | 0005267 | molecular_function | potassium channel activity |
| B | 0016020 | cellular_component | membrane |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
| C | 0005252 | molecular_function | open rectifier potassium channel activity |
| C | 0005267 | molecular_function | potassium channel activity |
| C | 0016020 | cellular_component | membrane |
| C | 0071805 | biological_process | potassium ion transmembrane transport |
| D | 0005252 | molecular_function | open rectifier potassium channel activity |
| D | 0005267 | molecular_function | potassium channel activity |
| D | 0016020 | cellular_component | membrane |
| D | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue K A 301 |
| Chain | Residue |
| A | ILE94 |
| B | GLY201 |
| A | GLY95 |
| A | ILE200 |
| A | GLY201 |
| A | K303 |
| A | K309 |
| B | ILE94 |
| B | GLY95 |
| B | ILE200 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue K A 303 |
| Chain | Residue |
| A | THR93 |
| A | ILE94 |
| A | THR199 |
| A | ILE200 |
| A | K301 |
| A | K304 |
| B | THR93 |
| B | ILE94 |
| B | THR199 |
| B | ILE200 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K A 304 |
| Chain | Residue |
| A | THR93 |
| A | THR199 |
| A | K303 |
| B | THR93 |
| B | THR199 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue Y01 A 305 |
| Chain | Residue |
| A | ARG3 |
| A | PHE246 |
| B | LEU115 |
| B | PRO119 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue Y01 A 306 |
| Chain | Residue |
| A | PHE80 |
| A | ALA81 |
| A | PHE84 |
| A | GLN215 |
| A | PHE225 |
| B | PHE16 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue DMU A 307 |
| Chain | Residue |
| A | ARG131 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue PC1 A 308 |
| Chain | Residue |
| A | LEU29 |
| B | ALA176 |
| B | HIS180 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue K A 309 |
| Chain | Residue |
| A | GLY95 |
| A | TYR96 |
| A | GLY201 |
| A | PHE202 |
| A | K301 |
| B | GLY95 |
| B | TYR96 |
| B | GLY201 |
| B | PHE202 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue KKQ A 300 |
| Chain | Residue |
| A | THR92 |
| A | THR93 |
| A | ILE118 |
| A | LEU122 |
| A | PHE125 |
| A | LEU197 |
| A | THR198 |
| A | THR199 |
| A | LEU232 |
| A | ILE235 |
| A | LEU239 |
| B | THR92 |
| B | THR93 |
| B | ILE118 |
| B | LEU122 |
| B | PHE125 |
| B | LEU197 |
| B | THR198 |
| B | THR199 |
| B | LEU232 |
| B | ILE235 |
| B | LEU239 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue Y01 B 302 |
| Chain | Residue |
| A | LEU115 |
| B | ARG3 |
| B | PHE246 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue Y01 B 303 |
| Chain | Residue |
| A | PHE16 |
| B | ARG79 |
| B | PHE80 |
| B | ALA81 |
| B | PHE84 |
| B | GLN215 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue DMU B 304 |
| Chain | Residue |
| B | ARG131 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue K C 301 |
| Chain | Residue |
| C | GLY95 |
| C | TYR96 |
| C | GLY201 |
| C | PHE202 |
| C | K302 |
| D | GLY95 |
| D | TYR96 |
| D | GLY201 |
| D | PHE202 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue K C 302 |
| Chain | Residue |
| C | ILE94 |
| C | GLY95 |
| C | ILE200 |
| C | GLY201 |
| C | K301 |
| C | K303 |
| D | ILE94 |
| D | GLY95 |
| D | ILE200 |
| D | GLY201 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue K C 303 |
| Chain | Residue |
| C | THR93 |
| C | ILE94 |
| C | THR199 |
| C | ILE200 |
| C | K302 |
| C | K304 |
| D | THR93 |
| D | ILE94 |
| D | THR199 |
| D | ILE200 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue K C 304 |
| Chain | Residue |
| C | THR93 |
| C | THR199 |
| C | K303 |
| D | THR93 |
| D | THR199 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue Y01 C 305 |
| Chain | Residue |
| C | ARG3 |
| C | PHE238 |
| C | PHE246 |
| D | LEU115 |
| site_id | AD9 |
| Number of Residues | 22 |
| Details | binding site for residue KKQ C 306 |
| Chain | Residue |
| C | THR92 |
| C | THR93 |
| C | ILE118 |
| C | LEU122 |
| C | PHE125 |
| C | LEU197 |
| C | THR198 |
| C | THR199 |
| C | LEU232 |
| C | ILE235 |
| C | LEU239 |
| D | THR92 |
| D | THR93 |
| D | ILE118 |
| D | LEU122 |
| D | PHE125 |
| D | LEU197 |
| D | THR198 |
| D | THR199 |
| D | LEU232 |
| D | ILE235 |
| D | LEU239 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue DMU C 307 |
| Chain | Residue |
| C | ARG131 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue PC1 D 701 |
| Chain | Residue |
| C | PHE112 |
| C | PHE186 |
| D | VAL25 |
| D | ALA28 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue Y01 D 702 |
| Chain | Residue |
| C | LEU115 |
| D | ARG3 |
| D | PHE246 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue Y01 D 703 |
| Chain | Residue |
| C | PHE16 |
| D | ARG79 |
| D | PHE80 |
| D | ALA81 |
| D | PHE84 |
| D | GLN215 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue DMU D 704 |
| Chain | Residue |
| C | GLU254 |
| D | ARG131 |
| D | LEU135 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue PC1 D 705 |
| Chain | Residue |
| C | LEU29 |
| D | GLY105 |
| D | PHE112 |
| D | SER169 |
| D | HIS180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 144 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | MET1-THR8 | |
| A | GLY129-ASN158 | |
| B | MET1-THR8 | |
| B | GLY129-ASN158 | |
| C | MET1-THR8 | |
| C | GLY129-ASN158 | |
| D | MET1-THR8 | |
| D | GLY129-ASN158 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 320 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU9-LEU29 | |
| C | VAL108-LEU128 | |
| C | MET159-SER179 | |
| C | PHE223-VAL243 | |
| D | LEU9-LEU29 | |
| D | VAL108-LEU128 | |
| D | MET159-SER179 | |
| D | PHE223-VAL243 | |
| A | VAL108-LEU128 | |
| A | MET159-SER179 | |
| A | PHE223-VAL243 | |
| B | LEU9-LEU29 | |
| B | VAL108-LEU128 | |
| B | MET159-SER179 | |
| B | PHE223-VAL243 | |
| C | LEU9-LEU29 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 92 |
| Details | INTRAMEM: Pore-forming; Name=Pore-forming 1 => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP78-PRO101 | |
| B | TRP78-PRO101 | |
| C | TRP78-PRO101 | |
| D | TRP78-PRO101 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 92 |
| Details | INTRAMEM: Pore-forming; Name=Pore-forming 2 => ECO:0000255 |
| Chain | Residue | Details |
| A | TRP184-ALA207 | |
| B | TRP184-ALA207 | |
| C | TRP184-ALA207 | |
| D | TRP184-ALA207 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN53 | |
| B | ASN53 | |
| C | ASN53 | |
| D | ASN53 |
