6IYU
Crystal Structure Analysis of an Eukaryotic Membrane Protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0014808 | biological_process | release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| A | 0016020 | cellular_component | membrane |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051279 | biological_process | regulation of release of sequestered calcium ion into cytosol |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | GLY74 |
| A | GLY74 |
| A | GLY74 |
| A | HOH523 |
| A | HOH523 |
| A | HOH523 |
| A | HOH553 |
| A | HOH553 |
| A | HOH553 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | TYR141 |
| A | HIS143 |
| A | GLY144 |
| A | HOH540 |
| A | HOH540 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | GLY133 |
| A | LYS155 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | GLN167 |
| A | ARG170 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | PRO51 |
| A | PHE52 |
| A | HOH531 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | TYR66 |
| A | ALA132 |
| A | LYS155 |
| A | HOH564 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical;Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 23 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30770441","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6IYU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IYX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IZ0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IZ1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6IZF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NA73","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
