Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005267 | molecular_function | potassium channel activity |
A | 0016020 | cellular_component | membrane |
A | 0071805 | biological_process | potassium ion transmembrane transport |
B | 0005267 | molecular_function | potassium channel activity |
B | 0016020 | cellular_component | membrane |
B | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue Q6F A 401 |
Chain | Residue |
A | SER131 |
A | LYS271 |
A | VAL274 |
A | TRP275 |
A | ILE278 |
A | PHE134 |
A | GLY137 |
A | THR138 |
A | ILE148 |
A | VAL258 |
A | ALA259 |
A | GLY260 |
A | GLY261 |
site_id | AC2 |
Number of Residues | 1 |
Details | binding site for residue CD A 402 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue D12 A 403 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue D12 A 404 |
Chain | Residue |
A | LEU221 |
A | LEU225 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue R16 A 408 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue K A 410 |
Chain | Residue |
A | GLY144 |
A | PHE145 |
A | GLY253 |
A | PHE254 |
B | GLY144 |
B | PHE145 |
B | GLY253 |
B | PHE254 |
B | K412 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue K A 411 |
Chain | Residue |
A | THR142 |
A | ILE143 |
A | THR251 |
A | ILE252 |
A | K412 |
B | THR142 |
B | ILE143 |
B | THR251 |
B | ILE252 |
B | K412 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue K A 412 |
Chain | Residue |
A | THR142 |
A | THR251 |
A | K411 |
B | THR142 |
B | THR251 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue UND A 413 |
site_id | AD1 |
Number of Residues | 1 |
Details | binding site for residue CD B 401 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue CD B 402 |
Chain | Residue |
A | GLU309 |
A | HIS313 |
B | GLU309 |
B | HIS313 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue CD B 403 |
site_id | AD4 |
Number of Residues | 11 |
Details | binding site for residue Q6F B 404 |
Chain | Residue |
B | HIS126 |
B | SER131 |
B | PHE134 |
B | GLY137 |
B | ASN147 |
B | ALA259 |
B | GLY260 |
B | GLY261 |
B | VAL274 |
B | TRP275 |
B | ILE278 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue D12 B 405 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue LNK B 407 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue OCT B 408 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue R16 B 411 |
site_id | AD9 |
Number of Residues | 10 |
Details | binding site for residue K B 412 |
Chain | Residue |
A | ILE143 |
A | GLY144 |
A | ILE252 |
A | GLY253 |
A | K410 |
A | K411 |
B | ILE143 |
B | GLY144 |
B | ILE252 |
B | GLY253 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 160 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | VAL47-ALA67 | |
A | ILE157-VAL177 | |
A | ILE208-VAL228 | |
A | VAL273-GLY293 | |
B | VAL47-ALA67 | |
B | ILE157-VAL177 | |
B | ILE208-VAL228 | |
B | VAL273-GLY293 | |
site_id | SWS_FT_FI2 |
Number of Residues | 52 |
Details | INTRAMEM: Pore-forming; Name=Pore-forming 1 => ECO:0000255 |
Chain | Residue | Details |
A | LEU129-GLY155 | |
B | LEU129-GLY155 | |
site_id | SWS_FT_FI3 |
Number of Residues | 58 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | GLY178-ARG207 | |
B | GLY178-ARG207 | |
site_id | SWS_FT_FI4 |
Number of Residues | 60 |
Details | INTRAMEM: Pore-forming; Name=Pore-forming 2 => ECO:0000255 |
Chain | Residue | Details |
A | ALA238-ASP268 | |
B | ALA238-ASP268 | |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | SER95 | |
A | ALA119 | |
B | SER95 | |
B | ALA119 | |