9J2N
Cryo-EM structure of the human glucose transporter, GLUT7 in outward-facing open conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005353 | molecular_function | fructose transmembrane transporter activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008645 | biological_process | hexose transmembrane transport |
| A | 0015755 | biological_process | fructose transmembrane transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016324 | cellular_component | apical plasma membrane |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0046323 | biological_process | D-glucose import |
| A | 0051119 | molecular_function | sugar transmembrane transporter activity |
| A | 0055056 | molecular_function | D-glucose transmembrane transporter activity |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0070837 | biological_process | dehydroascorbic acid transport |
| A | 1904659 | biological_process | D-glucose transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS00216 |
| Number of Residues | 17 |
| Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SAVLVERLGRRhllla.G |
| Chain | Residue | Details |
| A | SER338-GLY354 |
| site_id | PS00217 |
| Number of Residues | 26 |
| Details | SUGAR_TRANSPORT_2 Sugar transport proteins signature 2. VlGVCaGIsysalpmYlgElapknlR |
| Chain | Residue | Details |
| A | VAL140-ARG165 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 166 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| A | MET1-PRO21 | |
| A | ASP100-THR107 | |
| A | ALA160-THR172 | |
| A | PRO220-ARG281 | |
| A | GLU343-LEU350 | |
| A | PRO401-ARG415 | |
| A | PRO467-PHE512 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 240 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | THR22-LEU42 | |
| A | TYR380-VAL400 | |
| A | ALA416-PHE436 | |
| A | TYR446-ILE466 | |
| A | CYS79-VAL99 | |
| A | LEU108-ALA128 | |
| A | VAL139-LEU159 | |
| A | GLU173-GLY193 | |
| A | PRO199-PHE219 | |
| A | TRP282-ILE302 | |
| A | TYR322-VAL342 | |
| A | LEU351-PHE371 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 81 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| A | SER43-SER78 | |
| A | LYS129-ARG138 | |
| A | ASN194-TRP198 | |
| A | ASN303-GLN321 | |
| A | GLN372-SER379 | |
| A | PRO437-ALA445 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11169 |
| Chain | Residue | Details |
| A | GLN294 | |
| A | ASN300 | |
| A | ASN331 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN57 |
