7D7F
Structure of PKD1L3-CTD/PKD2L1 in calcium-bound state
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 | 120 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F |
Chain | Residue | Details |
A | LYS1656-LEU1666 | |
C | TRP434-PHE454 | |
C | PHE480-PHE499 | |
C | GLY537-LEU557 | |
D | LEU104-SER124 | |
D | VAL357-LEU376 | |
D | VAL385-ILE405 | |
D | TRP434-PHE454 | |
D | PHE480-PHE499 | |
D | GLY537-LEU557 | |
A | SER1883-ALA1911 | |
A | GLN1921-LEU1939 | |
A | SER1971-PHE1992 | |
A | ILE2010-SER2034 | |
A | SER2068-SER2087 | |
C | LEU104-SER124 | |
C | VAL357-LEU376 | |
C | VAL385-ILE405 |
site_id | SWS_FT_FI2 |
Number of Residues | 277 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
A | PHE1667-ASP1882 | |
D | PHE406-PHE433 | |
D | GLY500-LYS511 | |
D | ASN527-LEU536 | |
A | ILE1940-ILE1970 | |
A | TYR2035-THR2067 | |
B | ASN527-LEU536 | |
C | SER125-GLU356 | |
C | PHE406-PHE433 | |
C | GLY500-LYS511 | |
C | ASN527-LEU536 | |
D | SER125-GLU356 |
site_id | SWS_FT_FI3 |
Number of Residues | 77 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | PHE1912-ARG1920 | |
A | ALA1993-VAL2009 | |
A | SER2088-PRO2141 | |
C | LYS455-GLY479 | |
D | HIS377-SER384 | |
D | LYS455-GLY479 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc) asparagine => ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F |
Chain | Residue | Details |
A | LYS1702 | |
A | GLY1812 | |
D | CYS512-TYR526 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34381056, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F |
Chain | Residue | Details |
B | GLU370 | |
D | GLU373 | |
D | ASN387 | |
D | ASP390 | |
B | GLU373 | |
B | ASN387 | |
B | ASP390 | |
C | GLU370 | |
C | GLU373 | |
C | ASN387 | |
C | ASP390 | |
D | GLU370 |
site_id | SWS_FT_FI6 |
Number of Residues | 9 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29567962, ECO:0000269|PubMed:34381056, ECO:0007744|PDB:5Z1W, ECO:0007744|PDB:7D7E, ECO:0007744|PDB:7D7F |
Chain | Residue | Details |
B | ASN177 | |
B | ASN207 | |
B | ASN241 | |
C | ASN177 | |
C | ASN207 | |
C | ASN241 | |
D | ASN177 | |
D | ASN207 | |
D | ASN241 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN505 | |
C | ASN505 | |
D | ASN505 |