3UKM
Crystal structure of the human two pore domain potassium ion channel K2P1 (TWIK-1)
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 |
| C | 0005267 | molecular_function | potassium channel activity |
| C | 0016020 | cellular_component | membrane |
| C | 0071805 | biological_process | potassium ion transmembrane transport |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE K A 1 |
| Chain | Residue |
| A | K2 |
| A | GLY119 |
| A | TYR120 |
| A | GLY227 |
| A | LEU228 |
| B | GLY119 |
| B | TYR120 |
| B | GLY227 |
| B | LEU228 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE K A 2 |
| Chain | Residue |
| A | K1 |
| A | K3 |
| A | THR118 |
| A | GLY119 |
| A | ILE226 |
| A | GLY227 |
| B | THR118 |
| B | GLY119 |
| B | ILE226 |
| B | GLY227 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE K A 3 |
| Chain | Residue |
| A | K2 |
| A | K4 |
| A | THR117 |
| A | THR118 |
| A | THR225 |
| A | ILE226 |
| B | THR117 |
| B | THR118 |
| B | THR225 |
| B | ILE226 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 4 |
| Chain | Residue |
| A | K3 |
| A | THR117 |
| A | THR225 |
| B | THR117 |
| B | THR225 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE K C 1 |
| Chain | Residue |
| C | K2 |
| C | GLY119 |
| C | TYR120 |
| C | GLY227 |
| C | LEU228 |
| D | GLY119 |
| D | TYR120 |
| D | GLY227 |
| D | LEU228 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE K C 2 |
| Chain | Residue |
| C | K1 |
| C | K3 |
| C | THR118 |
| C | GLY119 |
| C | ILE226 |
| C | GLY227 |
| D | THR118 |
| D | GLY119 |
| D | ILE226 |
| D | GLY227 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE K C 3 |
| Chain | Residue |
| C | K2 |
| C | K4 |
| C | THR117 |
| C | THR118 |
| C | THR225 |
| C | ILE226 |
| D | THR117 |
| D | THR118 |
| D | THR225 |
| D | ILE226 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 4 |
| Chain | Residue |
| C | K3 |
| C | THR117 |
| C | THR225 |
| D | THR117 |
| D | THR225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 344 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | THR21-PHE41 | |
| C | PHE133-ILE156 | |
| C | VAL182-VAL202 | |
| C | LEU244-PHE267 | |
| D | THR21-PHE41 | |
| D | PHE133-ILE156 | |
| D | VAL182-VAL202 | |
| D | LEU244-PHE267 | |
| A | PHE133-ILE156 | |
| A | VAL182-VAL202 | |
| A | LEU244-PHE267 | |
| B | THR21-PHE41 | |
| B | PHE133-ILE156 | |
| B | VAL182-VAL202 | |
| B | LEU244-PHE267 | |
| C | THR21-PHE41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 244 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:22282804, ECO:0000305|PubMed:8978667 |
| Chain | Residue | Details |
| A | SER42-ASP103 | |
| B | SER42-ASP103 | |
| C | SER42-ASP103 | |
| D | SER42-ASP103 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 48 |
| Details | INTRAMEM: Helical; Name=Pore helix 1 => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | PHE104-SER116 | |
| B | PHE104-SER116 | |
| C | PHE104-SER116 | |
| D | PHE104-SER116 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | THR117-HIS122 | |
| A | THR225-TYR231 | |
| B | THR117-HIS122 | |
| B | THR225-TYR231 | |
| C | THR117-HIS122 | |
| C | THR225-TYR231 | |
| D | THR117-HIS122 | |
| D | THR225-TYR231 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 112 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | THR123-ALA132 | |
| D | THR123-ALA132 | |
| D | PHE203-ASN211 | |
| D | VAL232-GLU243 | |
| A | PHE203-ASN211 | |
| A | VAL232-GLU243 | |
| B | THR123-ALA132 | |
| B | PHE203-ASN211 | |
| B | VAL232-GLU243 | |
| C | THR123-ALA132 | |
| C | PHE203-ASN211 | |
| C | VAL232-GLU243 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 96 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | THR157-ILE181 | |
| B | THR157-ILE181 | |
| C | THR157-ILE181 | |
| D | THR157-ILE181 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 48 |
| Details | INTRAMEM: Helical; Name=Pore helix 2 => ECO:0000269|PubMed:22282804 |
| Chain | Residue | Details |
| A | PHE212-SER224 | |
| B | PHE212-SER224 | |
| C | PHE212-SER224 | |
| D | PHE212-SER224 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Important for increased permeability to Na(+) when K(+) levels are subphysiological => ECO:0000269|PubMed:21653227 |
| Chain | Residue | Details |
| A | THR118 | |
| B | THR118 | |
| C | THR118 | |
| D | THR118 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | SITE: Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability => ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:25001086 |
| Chain | Residue | Details |
| A | LEU146 | |
| B | LEU146 | |
| C | LEU146 | |
| D | LEU146 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | SITE: Part of a hydrophobic barrier that is stochastically dewetted and limits ion permeability => ECO:0000269|PubMed:25001086 |
| Chain | Residue | Details |
| A | LEU261 | |
| B | LEU261 | |
| C | LEU261 | |
| D | LEU261 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8978667 |
| Chain | Residue | Details |
| A | GLN95 | |
| B | GLN95 | |
| C | GLN95 | |
| D | GLN95 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:15820677, ECO:0000269|PubMed:20498050 |
| Chain | Residue | Details |
| A | LYS274 | |
| B | LYS274 | |
| C | LYS274 | |
| D | LYS274 |
