7D2K
Crystal structure of rat TRPV6 in complex with (4- phenylcyclohexyl)piperazine inhibitor Br-cis-22a
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005262 | molecular_function | calcium channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006816 | biological_process | calcium ion transport |
A | 0016020 | cellular_component | membrane |
A | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 122 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326 |
Chain | Residue | Details |
A | TYR327-VAL347 | |
A | LEU385-PHE407 | |
A | PRO423-ARG442 | |
A | GLU449-ALA468 | |
A | LEU489-PHE511 | |
A | ILE556-MET576 |
site_id | SWS_FT_FI2 |
Number of Residues | 63 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326 |
Chain | Residue | Details |
A | TYR348-ARG384 | |
A | LEU443-GLY448 | |
A | GLN512-ASP524 | |
A | ASN545-SER555 |
site_id | SWS_FT_FI3 |
Number of Residues | 33 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326 |
Chain | Residue | Details |
A | ARG408-GLY422 | |
A | ARG469-ASP488 |
site_id | SWS_FT_FI4 |
Number of Residues | 19 |
Details | INTRAMEM: Pore-forming => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326 |
Chain | Residue | Details |
A | TYR525-ALA544 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27296226, ECO:0007744|PDB:5IWK, ECO:0007744|PDB:5IWP |
Chain | Residue | Details |
A | ASP541 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:17197020 |
Chain | Residue | Details |
A | TYR161 | |
A | TYR162 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN357 |