7AWQ
Structure of the thermostabilized EAAT1 cryst-E386Q mutant in complex with L-ASP, sodium ions and the allosteric inhibitor UCPH101
Functional Information from GO Data
Functional Information from PROSITE/UniProt
| site_id | PS00713 |
| Number of Residues | 15 |
| Details | NA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GElLMrMLKMLIlP |
| Chain | Residue | Details |
| A | PRO84-PRO98 |
| site_id | PS00714 |
| Number of Residues | 24 |
| Details | NA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PvGaTiNMDGTaLYqaVaaIFIAQ |
| Chain | Residue | Details |
| A | PRO372-GLN395 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 122 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | MET1-ARG47 | |
| A | ALA109-ARG122 | |
| A | GLY241-ASP249 | |
| A | GLU357-ARG365 | |
| A | GLU475-MET522 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | ASN48-LEU68 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 61 |
| Details | TOPO_DOM: Extracellular => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | ARG69-GLU86 | |
| A | ALA278-MET298 | |
| A | ILE393-GLN405 | |
| A | LEU440-ASP452 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | LEU87-LEU108 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | ALA123-ILE145 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 27 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | PHE250-ILE277 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | VAL299-ILE320 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | THR321-PRO325 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 63 |
| Details | INTRAMEM: Discontinuously helical => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | PHE326-LEU356 | |
| A | ILE406-GLY439 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | ILE366-PHE392 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:28424515 |
| Chain | Residue | Details |
| A | TRP453-VAL474 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28424515, ECO:0007744|PDB:5LM4 |
| Chain | Residue | Details |
| A | THR382 | |
| A | ILE423 | |
| A | ASP456 | |
| A | THR376 | |
| A | SER343 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O59010 |
| Chain | Residue | Details |
| A | ASN378 | |
| A | ASN463 | |
| A | ASP467 | |
| A | GLY374 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER492 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | THR155 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
| Chain | Residue | Details |
| A | THR204 |
