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 | 3 |
Details | binding site for residue R2R A 401 |
Chain | Residue |
A | VAL107 |
A | ASP110 |
B | ASP110 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue D12 A 402 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue HEX A 404 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue K A 405 |
Chain | Residue |
A | PHE254 |
B | GLY144 |
B | PHE145 |
B | GLY253 |
B | PHE254 |
B | K402 |
A | GLY144 |
A | PHE145 |
A | GLY253 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue K A 406 |
Chain | Residue |
A | THR142 |
A | ILE143 |
A | THR251 |
A | ILE252 |
B | THR142 |
B | ILE143 |
B | THR251 |
B | ILE252 |
B | K402 |
B | K403 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CD A 410 |
Chain | Residue |
A | GLU309 |
A | HIS313 |
B | GLU309 |
B | HIS313 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CD B 401 |
Chain | Residue |
B | HIS126 |
B | ASP263 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue K B 402 |
Chain | Residue |
A | ILE143 |
A | GLY144 |
A | ILE252 |
A | GLY253 |
A | K405 |
A | K406 |
B | ILE143 |
B | GLY144 |
B | ILE252 |
B | GLY253 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue K B 403 |
Chain | Residue |
A | THR142 |
A | THR251 |
A | K406 |
B | THR142 |
B | THR251 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for Di-peptide OCT B 405 and ASP B 100 |
Chain | Residue |
B | ARG84 |
B | ASP96 |
B | GLU98 |
B | LEU99 |
B | GLU101 |
B | LEU102 |
B | ILE103 |
B | GLN104 |
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 | |