7WGD
X-ray structure of thermostabilized Drosophila dopamine transporter with GABA transporter1-like substitutions in the binding site, in substrate-free form.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| L | TYR193-HIS199 |
| site_id | PS00610 |
| Number of Residues | 15 |
| Details | NA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcykNGGGaF |
| Chain | Residue | Details |
| A | TRP51-PHE65 |
| site_id | PS00754 |
| Number of Residues | 21 |
| Details | NA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. FFfaSFTnsLPWtsCnniwNT |
| Chain | Residue | Details |
| A | PHE134-THR154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | VAL34-LYS59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 164 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | ASN60-GLY63 | |
| A | PHE139-LEU276 | |
| A | GLY326-SER349 | |
| A | TRP406-GLU445 | |
| A | ARG508 | |
| A | ARG589-THR591 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | ALA64-LEU87 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 69 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | GLY88-LYS107 | |
| A | THR298-ASN300 | |
| A | VAL376-VAL381 | |
| A | HIS472-ALA486 | |
| A | VAL536-GLY565 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 30 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | GLY108-SER138 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | LEU277-LEU297 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25961798, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | PHE301-LEU325 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | PHE350-GLY375 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | ALA382-PHE405 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | LEU446-PHE471 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | VAL487-ILE507 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | ASP509-THR535 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| A | SER566-GLN588 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24037379, ECO:0000269|PubMed:25970245, ECO:0007744|PDB:4XP1 |
| Chain | Residue | Details |
| A | GLY42 | |
| A | ALA44 | |
| A | VAL45 | |
| A | ASN49 | |
| A | PHE361 | |
| A | TYR393 | |
| A | VAL458 | |
| A | ALA461 | |
| A | SER462 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4XP1 |
| Chain | Residue | Details |
| A | GLY46 | |
| A | SER117 | |
| A | ASN121 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; atypical => ECO:0000269|PubMed:25970245, ECO:0007744|PDB:4XP1 |
| Chain | Residue | Details |
| A | ASN141 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 7 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
| Chain | Residue | Details |
| A | VAL205 | |
| A | GLU214 | |
| A | LEU223 | |
| A | ILE229 | |
| A | ALA234 | |
| A | VAL265 | |
| A | VAL341 |
