Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue PT5 A 301 |
| Chain | Residue |
| A | LEU64 |
| A | ACT304 |
| A | DMU312 |
| A | HOH418 |
| A | HOH428 |
| A | LEU68 |
| A | ILE85 |
| A | LYS130 |
| A | ARG134 |
| A | ALA165 |
| A | SER167 |
| A | GLY168 |
| A | THR195 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CPL A 302 |
| Chain | Residue |
| A | TYR103 |
| A | TYR107 |
| A | ARG115 |
| A | DMU309 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | HIS136 |
| A | HOH461 |
| A | HOH463 |
| A | HOH480 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | LYS171 |
| A | PT5301 |
| A | ACT305 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 305 |
| Chain | Residue |
| A | SER42 |
| A | HIS45 |
| A | ASP46 |
| A | ACT304 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 306 |
| Chain | Residue |
| A | HOH426 |
| A | HOH445 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue ACT A 307 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 308 |
| Chain | Residue |
| A | LEU41 |
| A | THR118 |
| A | HOH434 |
| A | HOH435 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue DMU A 309 |
| Chain | Residue |
| A | TYR28 |
| A | LEU96 |
| A | CPL302 |
| A | HOH410 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue DMU A 311 |
| Chain | Residue |
| A | TYR30 |
| A | ARG115 |
| A | LEU116 |
| A | ALA117 |
| A | TRP119 |
| A | HOH408 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue DMU A 312 |
| Chain | Residue |
| A | PHE54 |
| A | HIS58 |
| A | PHE60 |
| A | SER61 |
| A | TRP63 |
| A | LEU64 |
| A | LEU158 |
| A | ALA177 |
| A | THR195 |
| A | LYS196 |
| A | VAL199 |
| A | PT5301 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for Poly-Saccharide residues TYR A 21 through DMU A 310 |
| Chain | Residue |
| A | ASP17 |
| A | ALA18 |
| A | GLY19 |
| A | GLY20 |
| A | VAL22 |
| A | GLN23 |
| A | LYS24 |
| A | LEU25 |
| A | LYS26 |
| A | TYR30 |
| A | PHE31 |
| A | GLY125 |
Functional Information from PROSITE/UniProt
| site_id | PS00626 |
| Number of Residues | 11 |
| Details | RCC1_2 Regulator of chromosome condensation (RCC1) signature 2. IAAGvKHAVRI |
| Chain | Residue | Details |
| A | ILE138-ILE148 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical;Name=1","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Discontinuously helical;Name=2","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical;Name=3","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 30 |
| Details | Transmembrane: {"description":"Helical;Name=4","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Discontinuously helical;Name=5","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical;Name=6","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical;Name=7","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5EIK","evidenceCode":"ECO:0007744"}]} |