8XVX
Cryo-EM structure of OSCA1.2-DOPC-1:20-expanded state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005227 | molecular_function | calcium-activated cation channel activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006812 | biological_process | monoatomic cation transport |
| A | 0008381 | molecular_function | mechanosensitive monoatomic ion channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0098655 | biological_process | monoatomic cation transmembrane transport |
| B | 0005227 | molecular_function | calcium-activated cation channel activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006812 | biological_process | monoatomic cation transport |
| B | 0008381 | molecular_function | mechanosensitive monoatomic ion channel activity |
| B | 0016020 | cellular_component | membrane |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0098655 | biological_process | monoatomic cation transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS01319 |
| Number of Residues | 22 |
| Details | RBFA Ribosome-binding factor A signature. VQSlAtiegi.VKaAPFLkFivD |
| Chain | Residue | Details |
| B | VAL396-ASP417 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 224 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:30382939 |
| Chain | Residue | Details |
| B | MET1-ASP6 | |
| A | GLN489-ALA526 | |
| A | MET589-LEU591 | |
| A | THR648-HIS650 | |
| B | PRO122-ARG158 | |
| B | GLN397-GLY427 | |
| B | GLN489-ALA526 | |
| B | MET589-LEU591 | |
| B | THR648-HIS650 | |
| A | MET1-ASP6 | |
| A | PRO122-ARG158 | |
| A | GLN397-GLY427 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 440 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| B | ILE7-VAL27 | |
| B | VAL627-GLY647 | |
| B | ALA651-PHE671 | |
| A | ILE7-VAL27 | |
| A | ILE101-VAL121 | |
| A | PHE159-LYS179 | |
| A | LEU376-VAL396 | |
| A | PHE428-MET448 | |
| A | TYR468-GLU488 | |
| A | GLY527-PHE547 | |
| A | THR568-PRO588 | |
| B | ILE101-VAL121 | |
| A | PRO592-VAL612 | |
| A | VAL627-GLY647 | |
| A | ALA651-PHE671 | |
| B | PHE159-LYS179 | |
| B | LEU376-VAL396 | |
| B | PHE428-MET448 | |
| B | TYR468-GLU488 | |
| B | GLY527-PHE547 | |
| B | THR568-PRO588 | |
| B | PRO592-VAL612 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 832 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30382939 |
| Chain | Residue | Details |
| B | LEU28-ARG100 | |
| A | LEU548-ASN567 | |
| A | TYR613-ASP626 | |
| A | CYS672-VAL771 | |
| B | GLU180-ARG375 | |
| B | SER449-ARG467 | |
| B | LEU548-ASN567 | |
| B | TYR613-ASP626 | |
| B | CYS672-VAL771 | |
| A | LEU28-ARG100 | |
| A | GLU180-ARG375 | |
| A | SER449-ARG467 |
