7S8C
Cryo-EM structure of human TRPV6 in complex with inhibitor econazole
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 |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005262 | molecular_function | calcium channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006816 | biological_process | calcium ion transport |
B | 0016020 | cellular_component | membrane |
B | 0055085 | biological_process | transmembrane transport |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005262 | molecular_function | calcium channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006816 | biological_process | calcium ion transport |
C | 0016020 | cellular_component | membrane |
C | 0055085 | biological_process | transmembrane transport |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0005262 | molecular_function | calcium channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0006816 | biological_process | calcium ion transport |
D | 0016020 | cellular_component | membrane |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 488 |
Details | TRANSMEM: Helical => ECO:0000305|PubMed:29258289 |
Chain | Residue | Details |
A | TYR328-ILE348 | |
B | GLU450-ALA469 | |
B | LEU490-PHE512 | |
B | ILE557-MET577 | |
C | TYR328-ILE348 | |
C | LEU386-PHE408 | |
C | PRO424-ARG443 | |
C | GLU450-ALA469 | |
C | LEU490-PHE512 | |
C | ILE557-MET577 | |
D | TYR328-ILE348 | |
A | LEU386-PHE408 | |
D | LEU386-PHE408 | |
D | PRO424-ARG443 | |
D | GLU450-ALA469 | |
D | LEU490-PHE512 | |
D | ILE557-MET577 | |
A | PRO424-ARG443 | |
A | GLU450-ALA469 | |
A | LEU490-PHE512 | |
A | ILE557-MET577 | |
B | TYR328-ILE348 | |
B | LEU386-PHE408 | |
B | PRO424-ARG443 |
site_id | SWS_FT_FI2 |
Number of Residues | 252 |
Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:29258289 |
Chain | Residue | Details |
A | TYR349-ARG385 | |
C | LEU444-GLY449 | |
C | GLN513-ASP525 | |
C | ASN546-SER556 | |
D | TYR349-ARG385 | |
D | LEU444-GLY449 | |
D | GLN513-ASP525 | |
D | ASN546-SER556 | |
A | LEU444-GLY449 | |
A | GLN513-ASP525 | |
A | ASN546-SER556 | |
B | TYR349-ARG385 | |
B | LEU444-GLY449 | |
B | GLN513-ASP525 | |
B | ASN546-SER556 | |
C | TYR349-ARG385 |
site_id | SWS_FT_FI3 |
Number of Residues | 132 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:29258289 |
Chain | Residue | Details |
A | ARG409-GLY423 | |
A | ARG470-ASP489 | |
B | ARG409-GLY423 | |
B | ARG470-ASP489 | |
C | ARG409-GLY423 | |
C | ARG470-ASP489 | |
D | ARG409-GLY423 | |
D | ARG470-ASP489 |
site_id | SWS_FT_FI4 |
Number of Residues | 76 |
Details | INTRAMEM: Pore-forming => ECO:0000305|PubMed:29258289 |
Chain | Residue | Details |
A | TYR526-ALA545 | |
B | TYR526-ALA545 | |
C | TYR526-ALA545 | |
D | TYR526-ALA545 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:29258289 |
Chain | Residue | Details |
A | ASP542 | |
B | ASP542 | |
C | ASP542 | |
D | ASP542 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:Q9R186 |
Chain | Residue | Details |
A | TYR161 | |
B | TYR161 | |
C | TYR161 | |
D | TYR161 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN358 | |
B | ASN358 | |
C | ASN358 | |
D | ASN358 |