7WGD
X-ray structure of thermostabilized Drosophila dopamine transporter with GABA transporter1-like substitutions in the binding site, in substrate-free form.
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Sodium-dependent dopamine transporter | polymer | 536 | 60144.6 | 1 | UniProt (Q7K4Y6) Pfam (PF00209) In PDB | Drosophila melanogaster (fruit fly) | Protein fumin |
| 2 | L | Antibody fragment (9D5) Light Chain | polymer | 214 | 23306.6 | 1 | Mus musculus | ||
| 3 | H | Antibody fragment (9D5) heavy chain | polymer | 219 | 23619.4 | 1 | Mus musculus | ||
| 4 | A | SODIUM ION | non-polymer | 23.0 | 2 | Chemie (NA) | |||
| 5 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 6 | A | CHOLESTEROL HEMISUCCINATE | non-polymer | 486.7 | 1 | Chemie (Y01) | |||
| 7 | A | CHOLESTEROL | non-polymer | 386.7 | 1 | Chemie (CLR) | |||
| 8 | water | water | 18.0 | 19 | Chemie (HOH) |
Sequence modifications
A: 25 - 601 (UniProt: Q7K4Y6)
| PDB | External Database | Details |
|---|---|---|
| Tyr 43 | Phe 43 | engineered mutation |
| Gly 46 | Asp 46 | engineered mutation |
| Ala 74 | Val 74 | engineered mutation |
| Ser 117 | Ala 117 | engineered mutation |
| Leu 120 | Val 120 | engineered mutation |
| Asn 121 | Asp 121 | engineered mutation |
| - | Ser 162 | deletion |
| - | Gln 163 | deletion |
| - | Asn 164 | deletion |
| - | Ala 165 | deletion |
| - | Ser 166 | deletion |
| - | Arg 167 | deletion |
| - | Val 168 | deletion |
| - | Pro 169 | deletion |
| - | Val 170 | deletion |
| - | Ile 171 | deletion |
| - | Gly 172 | deletion |
| - | Asn 173 | deletion |
| - | Tyr 174 | deletion |
| - | Ser 175 | deletion |
| - | Asp 176 | deletion |
| - | Leu 177 | deletion |
| - | Tyr 178 | deletion |
| - | Ala 179 | deletion |
| - | Met 180 | deletion |
| - | Gly 181 | deletion |
| - | Asn 182 | deletion |
| - | Gln 183 | deletion |
| - | Ser 184 | deletion |
| - | Leu 185 | deletion |
| - | Leu 186 | deletion |
| - | Tyr 187 | deletion |
| - | Asn 188 | deletion |
| - | Glu 189 | deletion |
| - | Thr 190 | deletion |
| - | Tyr 191 | deletion |
| - | Met 192 | deletion |
| - | Asn 193 | deletion |
| - | Gly 194 | deletion |
| - | Ser 195 | deletion |
| - | Ser 196 | deletion |
| - | Leu 197 | deletion |
| - | Asp 198 | deletion |
| - | Thr 199 | deletion |
| - | Ser 200 | deletion |
| - | Ala 201 | deletion |
| - | Val 202 | deletion |
| Ala 275 | Val 275 | engineered mutation |
| Ala 311 | Val 311 | engineered mutation |
| Leu 325 | Phe 325 | engineered mutation |
| Ser 327 | Val 327 | engineered mutation |
| Ser 384 | Glu 384 | engineered mutation |
| Ala 415 | Leu 415 | engineered mutation |
| Gln 422 | Ser 422 | engineered mutation |
| Thr 425 | Gly 425 | engineered mutation |
| Val 426 | Ser 426 | engineered mutation |
| Leu 538 | Gly 538 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 3 |
| Total formula weight | 107070.6 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 954.8 | |
| All* | Total formula weight | 108025.4 |
