8Y66
Cryo-EM structure of human urate transporter GLUT9 bound to inhibitor apigenin
Functional Information from PROSITE/UniProt
site_id | PS00216 |
Number of Residues | 17 |
Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SGLVIEHLGRRpllig.G |
Chain | Residue | Details |
A | SER371-GLY387 |
site_id | PS00217 |
Number of Residues | 26 |
Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. ImGIDgGValsvlpmYlsEispkeiR |
Chain | Residue | Details |
A | ILE173-ARG198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | TRP52-GLY72 |
site_id | SWS_FT_FI2 |
Number of Residues | 85 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | TYR73-THR107 | |
A | GLY162-ARG171 | |
A | PRO222-TRP231 | |
A | TYR338-PRO354 | |
A | THR403-SER415 | |
A | GLN473-THR478 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | LEU108-VAL128 |
site_id | SWS_FT_FI4 |
Number of Residues | 140 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | LYS129-THR140 | |
A | SER193-SER200 | |
A | PRO253-GLN316 | |
A | GLU376-ARG381 | |
A | LEU437-PHE451 | |
A | PRO500-PRO540 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | LEU141-ALA161 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | PHE172-ILE192 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | LEU201-LEU221 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | PRO232-LEU252 |
site_id | SWS_FT_FI9 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | VAL317-PHE337 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000255 |
Chain | Residue | Details |
A | TYR355-ILE375 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000255 |
Chain | Residue | Details |
A | PRO382-LEU402 |
site_id | SWS_FT_FI12 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=10 => ECO:0000255 |
Chain | Residue | Details |
A | ILE416-ILE436 |
site_id | SWS_FT_FI13 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=11 => ECO:0000255 |
Chain | Residue | Details |
A | ILE452-ILE472 |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=12 => ECO:0000255 |
Chain | Residue | Details |
A | TYR479-LEU499 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER9 | |
A | SER515 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN90 |