5K47
CryoEM structure of the human Polycystin-2/PKD2 TRP channel
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0016020 | cellular_component | membrane |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0016020 | cellular_component | membrane |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0016020 | cellular_component | membrane |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0016020 | cellular_component | membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | VAL220-MET241 | |
| B | VAL220-MET241 | |
| C | VAL220-MET241 | |
| D | VAL220-MET241 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1076 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | MET242-THR468 | |
| C | TYR527-ALA552 | |
| C | GLY620-GLU631 | |
| C | ALA647-ARG654 | |
| D | MET242-THR468 | |
| D | TYR527-ALA552 | |
| D | GLY620-GLU631 | |
| D | ALA647-ARG654 | |
| A | TYR527-ALA552 | |
| A | GLY620-GLU631 | |
| A | ALA647-ARG654 | |
| B | MET242-THR468 | |
| B | TYR527-ALA552 | |
| B | GLY620-GLU631 | |
| B | ALA647-ARG654 | |
| C | MET242-THR468 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | PHE469-VAL489 | |
| B | PHE469-VAL489 | |
| C | PHE469-VAL489 | |
| D | PHE469-VAL489 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 152 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | GLU490-SER505 | |
| A | PHE574-LEU597 | |
| B | GLU490-SER505 | |
| B | PHE574-LEU597 | |
| C | GLU490-SER505 | |
| C | PHE574-LEU597 | |
| D | GLU490-SER505 | |
| D | PHE574-LEU597 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | PHE506-ILE526 | |
| B | PHE506-ILE526 | |
| C | PHE506-ILE526 | |
| D | PHE506-ILE526 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | TYR553-LEU573 | |
| B | TYR553-LEU573 | |
| C | TYR553-LEU573 | |
| D | TYR553-LEU573 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | PHE598-PHE619 | |
| B | PHE598-PHE619 | |
| C | PHE598-PHE619 | |
| D | PHE598-PHE619 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 56 |
| Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | CYS632-PHE646 | |
| B | CYS632-PHE646 | |
| C | CYS632-PHE646 | |
| D | CYS632-PHE646 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | VAL655-MET675 | |
| B | VAL655-MET675 | |
| C | VAL655-MET675 | |
| D | VAL655-MET675 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | ASN299 | |
| A | ASN305 | |
| B | ASN299 | |
| B | ASN305 | |
| C | ASN299 | |
| C | ASN305 | |
| D | ASN299 | |
| D | ASN305 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | ASN328 | |
| B | ASN328 | |
| C | ASN328 | |
| D | ASN328 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368 |
| Chain | Residue | Details |
| A | ASN362 | |
| A | ASN375 | |
| B | ASN362 | |
| B | ASN375 | |
| C | ASN362 | |
| C | ASN375 | |
| D | ASN362 | |
| D | ASN375 |
