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 | 117 |
Details | TOPO_DOM: Lumenal => ECO:0000305|PubMed:27698420 |
Chain | Residue | Details |
A | MET1-TYR27 | |
C | GLY81-LYS89 | |
C | PRO149-ASN150 | |
C | THR211-ALA215 | |
A | GLY81-LYS89 | |
A | PRO149-ASN150 | |
A | THR211-ALA215 | |
B | MET1-TYR27 | |
B | GLY81-LYS89 | |
B | PRO149-ASN150 | |
B | THR211-ALA215 | |
C | MET1-TYR27 |
site_id | SWS_FT_FI2 |
Number of Residues | 51 |
Details | TRANSMEM: Helical;Name=1 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | PRO28-ASP45 | |
B | PRO28-ASP45 | |
C | PRO28-ASP45 |
site_id | SWS_FT_FI3 |
Number of Residues | 93 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:27698420 |
Chain | Residue | Details |
A | LEU46-LYS56 | |
A | PRO108-THR119 | |
A | GLY178-LEU188 | |
B | LEU46-LYS56 | |
B | PRO108-THR119 | |
B | GLY178-LEU188 | |
C | LEU46-LYS56 | |
C | PRO108-THR119 | |
C | GLY178-LEU188 |
site_id | SWS_FT_FI4 |
Number of Residues | 69 |
Details | TRANSMEM: Discontinuously helical;Name=2 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | HIS57-LEU80 | |
B | HIS57-LEU80 | |
C | HIS57-LEU80 |
site_id | SWS_FT_FI5 |
Number of Residues | 51 |
Details | TRANSMEM: Helical;Name=3 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | ARG90-ALA107 | |
B | ARG90-ALA107 | |
C | ARG90-ALA107 |
site_id | SWS_FT_FI6 |
Number of Residues | 84 |
Details | TRANSMEM: Helical;Name=4 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | PRO120-TYR148 | |
B | PRO120-TYR148 | |
C | PRO120-TYR148 |
site_id | SWS_FT_FI7 |
Number of Residues | 78 |
Details | TRANSMEM: Discontinuously helical;Name=5 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | SER151-ARG177 | |
B | SER151-ARG177 | |
C | SER151-ARG177 |
site_id | SWS_FT_FI8 |
Number of Residues | 63 |
Details | TRANSMEM: Helical;Name=6 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | ARG189-GLY210 | |
B | ARG189-GLY210 | |
C | ARG189-GLY210 |
site_id | SWS_FT_FI9 |
Number of Residues | 69 |
Details | TRANSMEM: Helical;Name=7 => ECO:0000269|PubMed:27698420 |
Chain | Residue | Details |
A | PRO216-HIS239 | |
B | PRO216-HIS239 | |
C | PRO216-HIS239 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27698420, ECO:0007744|PDB:5EGI |
Chain | Residue | Details |
A | LYS129 | |
A | ARG133 | |
B | LYS129 | |
B | ARG133 | |
C | LYS129 | |
C | ARG133 |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0007744|PDB:5EGI |
Chain | Residue | Details |
A | SER166 | |
B | SER166 | |
C | SER166 |