5EGI
Structure of a Trimeric Intracellular Cation channel from C. elegans with bound Ca2+
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 |
| B | 0005267 | molecular_function | potassium channel activity |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
| C | 0005267 | molecular_function | potassium channel activity |
| C | 0016020 | cellular_component | membrane |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue PT5 A 301 |
| Chain | Residue |
| A | GLU41 |
| A | HIS184 |
| A | GLU186 |
| A | PRO190 |
| A | SER191 |
| A | THR194 |
| B | SER60 |
| B | SER64 |
| B | ARG177 |
| A | MET68 |
| A | LYS129 |
| A | ARG133 |
| A | ALA164 |
| A | GLY165 |
| A | SER166 |
| A | GLY167 |
| A | ARG170 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue PT5 B 301 |
| Chain | Residue |
| B | GLU41 |
| B | LEU79 |
| B | LYS129 |
| B | ARG133 |
| B | ALA164 |
| B | SER166 |
| B | GLY167 |
| B | ILE168 |
| B | ARG170 |
| B | HIS184 |
| B | GLU186 |
| B | ALA193 |
| B | THR194 |
| C | LEU63 |
| C | LEU67 |
| C | PHE74 |
| C | ARG177 |
| C | DMU302 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 302 |
| Chain | Residue |
| B | HOH401 |
| B | HOH401 |
| B | HOH402 |
| B | HOH402 |
| C | HOH404 |
| C | HOH404 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue PT5 C 301 |
| Chain | Residue |
| A | LEU67 |
| A | LEU172 |
| C | GLU41 |
| C | MET68 |
| C | PHE78 |
| C | LYS129 |
| C | ARG133 |
| C | THR160 |
| C | ALA164 |
| C | GLY165 |
| C | SER166 |
| C | GLY167 |
| C | ILE168 |
| C | ARG170 |
| C | HIS184 |
| C | PRO190 |
| C | THR194 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue DMU C 302 |
| Chain | Residue |
| B | LEU157 |
| B | THR194 |
| B | VAL198 |
| B | PT5301 |
| C | PHE53 |
| C | HIS57 |
| C | LEU59 |
| C | SER60 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 51 |
| Details | Transmembrane: {"description":"Helical;Name=1","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 93 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 69 |
| Details | Transmembrane: {"description":"Discontinuously helical;Name=2","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 51 |
| Details | Transmembrane: {"description":"Helical;Name=3","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 84 |
| Details | Transmembrane: {"description":"Helical;Name=4","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 78 |
| Details | Transmembrane: {"description":"Discontinuously helical;Name=5","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 63 |
| Details | Transmembrane: {"description":"Helical;Name=6","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 69 |
| Details | Transmembrane: {"description":"Helical;Name=7","evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27698420","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5EGI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
