4XPT
X-ray structure of Drosophila dopamine transporter with subsiteB mutations D121G/S426M and EL2 deletion of 162-201 in complex with substrate analogue 3,4 dichlorophen ethylamine
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A | Dopamine transporter | polymer | 535 | 59977.5 | 1 | UniProt (Q7K4Y6) Pfam (PF00209) In PDB | Drosophila melanogaster (Fruit fly) | Dopamine transporter,isoform A,GH22929p |
| 2 | L | antibody fragment light chain | polymer | 214 | 23306.6 | 1 | Mus musculus | ||
| 3 | H | antibody fragment heavy chain | polymer | 219 | 23619.4 | 1 | Mus musculus | ||
| 4 | B, C, D, E, F | alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose | branched | 342.3 | 5 | In PDB BIRD (PRD_900018) GlyTouCan (G66120GK) | beta-maltose | ||
| 5 | A | CHOLESTEROL HEMISUCCINATE | non-polymer | 486.7 | 1 | Chemie (Y01) | |||
| 6 | A | 2-(3,4-dichlorophenyl)ethanamine | non-polymer | 190.1 | 1 | Chemie (42J) | |||
| 7 | A | 2-acetamido-2-deoxy-beta-D-glucopyranose | non-polymer | 221.2 | 1 | Chemie (NAG) | |||
| 8 | A | CHOLESTEROL | non-polymer | 386.7 | 1 | Chemie (CLR) | |||
| 9 | A | CHLORIDE ION | non-polymer | 35.5 | 1 | Chemie (CL) | |||
| 10 | A | SODIUM ION | non-polymer | 23.0 | 2 | Chemie (NA) |
Sequence modifications
A: 25 - 599 (UniProt: Q7K4Y6)
| 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 |
| 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 | 106903.5 | |
| Branched | Number of molecules | 5 |
| Total formula weight | 1711.5 | |
| Non-Polymers* | Number of molecules | 7 |
| Total formula weight | 1366.1 | |
| All* | Total formula weight | 109981.1 |
