4XPH
X-ray structure of Drosophila dopamine transporter with subsiteB mutations (D121G/S426M) bound to 3,4dichlorophenethylamine
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Transporter | polymer | 534 | 59878.4 | 1 | UniProt (Q9NB97) Pfam (PF00209) UniProt (by SIFTS) (Q7K4Y6) | Drosophila melanogaster (Fruit fly) | |
| 2 | B (L) | Antibody fragment light chain | polymer | 214 | 23320.6 | 1 | Mus musculus | ||
| 3 | C (H) | Antibody fragment heavy chain | polymer | 219 | 23619.4 | 1 | Mus musculus | ||
| 4 | D (B) | alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose | branched | 342.3 | 1 | In PDB BIRD (PRD_900018) GlyTouCan (G66120GK) | beta-maltose | ||
| 5 | E (A) | 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE | non-polymer | 162.2 | 1 | Chemie (P4G) | |||
| 6 | F (A) | 2-(3,4-dichlorophenyl)ethanamine | non-polymer | 190.1 | 1 | Chemie (42J) | |||
| 7 | G, H, L (A, L) | SODIUM ION | non-polymer | 23.0 | 3 | Chemie (NA) | |||
| 8 | I (A) | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 9 | J, K (A) | CHOLESTEROL | non-polymer | 386.7 | 2 | Chemie (CLR) | |||
| 10 | M, N, O (A, L, H) | water | water | 18.0 | 15 | Chemie (HOH) |
Sequence modifications
A: 25 - 599 (UniProt: Q9NB97)
| PDB | External Database | Details |
|---|---|---|
| Ala 74 | Val 74 | engineered mutation |
| Gly 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 415 | Leu 415 | engineered mutation |
| Met 426 | Ser 426 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 3 |
| Total formula weight | 106818.4 | |
| Branched | Number of molecules | 1 |
| Total formula weight | 342.3 | |
| Non-Polymers* | Number of molecules | 8 |
| Total formula weight | 1230.0 | |
| All* | Total formula weight | 108390.7 |
