Inhibitor-free outward-open structure of Drosophila dopamine transporter. Determined by electron microscopy at 3.0 Å resolution. Released 24 Jul 2024.
Explore 9EUP in 3D Show helices and sheets RCSB PDB PDBe
9EUP contains 51 α-helices and 52 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-44 | 12 | |
| α-helix | 48-51 | 4 | |
| α-helix | 53-59 | 7 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-72 | 7 | |
| α-helix | 73-77 | 5 | |
| α-helix | 78-91 | 14 | |
| α-helix | 95-102 | 8 | |
| α-helix | 104-107 | 4 | |
| α-helix | 108-137 | 30 | |
| α-helix | 144-146 | 3 | |
| β-strand | 157-158 | 2 | 1 |
| β-strand | 162 | 1 | 2 |
| β-strand | 208 | 1 | 2 |
| β-strand | 209-210 | 2 | 1 |
| α-helix | 211-215 | 5 | |
| α-helix | 216-220 | 5 | |
| α-helix | 223-225 | 3 | |
| β-strand | 235 | 1 | 3 |
| α-helix | 237-254 | 18 | |
| α-helix | 258-268 | 11 | |
| α-helix | 271-284 | 14 | |
| α-helix | 289-297 | 9 | |
| α-helix | 301-305 | 5 | |
| α-helix | 307-321 | 15 | |
| α-helix | 327-332 | 6 | |
| α-helix | 341-369 | 29 | |
| α-helix | 370-374 | 5 | |
| α-helix | 378-381 | 4 | |
| α-helix | 386-387 | 2 | |
| α-helix | 388-392 | 5 | |
| α-helix | 393-397 | 5 | |
| α-helix | 403-436 | 34 | |
| α-helix | 438-441 | 4 | |
| α-helix | 444-459 | 16 | |
| β-strand | 464 | 1 | 3 |
| α-helix | 467-477 | 11 | |
| α-helix | 481-492 | 12 | |
| α-helix | 493-499 | 7 | |
| α-helix | 500-511 | 12 | |
| α-helix | 514-516 | 3 | |
| α-helix | 517-521 | 5 | |
| α-helix | 522-526 | 5 | |
| α-helix | 527-540 | 14 | |
| β-strand | 546-547 | 2 | 4 |
| β-strand | 550-551 | 2 | 4 |
| α-helix | 554-581 | 28 | |
| α-helix | 586-594 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 5 |
| β-strand | 11-12 | 2 | 6 |
| β-strand | 18-25 | 8 | 5 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 7 |
| β-strand | 45-51 | 7 | 7 |
| β-strand | 58-60 | 3 | 7 |
| β-strand | 68-73 | 6 | 5 |
| β-strand | 78-83 | 6 | 5 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 7 |
| α-helix | 102-104 | 3 | |
| β-strand | 108-109 | 2 | 7 |
| β-strand | 113-115 | 3 | 7 |
| β-strand | 116-117 | 2 | 6 |
| α-helix | 120-122 | 3 | |
| β-strand | 123 | 1 | 8 |
| β-strand | 128-130 | 3 | 9 |
| β-strand | 141-151 | 11 | 9 |
| β-strand | 152 | 1 | 8 |
| β-strand | 157-160 | 4 | 10 |
| β-strand | 165 | 1 | 10 |
| β-strand | 169-171 | 3 | 9 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-177 | 3 | 9 |
| β-strand | 180-190 | 11 | 9 |
| β-strand | 200-205 | 6 | 10 |
| β-strand | 210-215 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 11 |
| β-strand | 10-12 | 3 | 12 |
| β-strand | 19-25 | 7 | 11 |
| α-helix | 28-30 | 3 | |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 46-50 | 5 | 12 |
| β-strand | 54-55 | 2 | 12 |
| β-strand | 63-68 | 6 | 11 |
| β-strand | 71-76 | 6 | 11 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 12 |
| β-strand | 99 | 1 | 12 |
| β-strand | 103-106 | 4 | 12 |
| β-strand | 112 | 1 | 13 |
| β-strand | 116-119 | 4 | 14 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-128 | 6 | |
| β-strand | 130-140 | 11 | 14 |
| β-strand | 141 | 1 | 13 |
| β-strand | 145-151 | 7 | 15 |
| β-strand | 154-156 | 3 | 15 |
| β-strand | 160-164 | 5 | 14 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 14 |
| α-helix | 184-189 | 6 | |
| β-strand | 192-199 | 8 | 15 |
| β-strand | 202-211 | 10 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium-dependent dopamine transporter | A | protein | 543 | Drosophila melanogaster | Q7K4Y6 (AlphaFold model) |
| 9D5 antibody, heavy chain | H | protein | 240 | Mus musculus | |
| 9D5 antibody, light chain | L | protein | 237 | Mus musculus |
>9EUP_1 Sodium-dependent dopamine transporter (chains A) MNSISDERETWSGKVDFLLSVIGFAVDLANVWRFPYLCYKNGGGAFLVPYGIMLAVGGIP LFYMELALGQHNRKGAITCWGRLVPLFKGIGYAVVLIAFYVDFYYNVIIAWSLRFFFASF TNSLPWTSCNNIWNTPNCRPFESQGFQSAASEYFNRYILELNRSEGIHDLGAIKWDMALC LLIVYLICYFSLWKGISTSGKVVWFTALFPYAALLILLIRGLTLPGSFLGIQYYLTPNFS AIYKAEVWADAATQVFFSLGPGFGVLLAYASYNKYHNNVYKDALLTSFINSATSFIAGFV IFSVLGYMAHTLGVRIEDVATEGPGLVFVVYPAAIATMPASTFWALIFFMMLATLGLDSS FGGSEAIITALSDEFPKIKRNRELFVAGLFSLYFVVGLASCTQGGFYFFHLLDRYAAGYS ILVAVFFEAIAVSWIYGTNRFSEDIRDMIGFPPGRYWQVCWRFVAPIFLLFITVYLLIGY EPLTYADYVYPSWANALGWCIAGSSVVMIPAVAIFKLLSTPGSLRQRFTILTTPWRDQQL VPR
>9EUP_2 9D5 ANTIBODY, HEAVY CHAIN (chains H) MNFGLRLVFLVLILKGVQCEVQLVESGGGLVKPGGSLKLSCAASGFTFSSYAMSWVRQSP EKRLEWVAEISSGGRYIYYSDTVTGRFTISRDNARNILHLEMSSLRSEDTAMYYCARGEV RQRGFDYWGQGTTLTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWN SGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGP
>9EUP_3 9D5 ANTIBODY, LIGHT CHAIN (chains L) MDFQVQIFSFLLISASVAMSRGENVLTQSPAIMSTSPGEKVTMTCRASSSVGSSYLHWYQ QKSGASPKLWIYSTSNLASGVPARFSGSGSGTSYSLTISSVEAEDAATYYCQQFSGYPLT FGSGTKLEMKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQN GVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
| ID | Name | Formula | Copies |
|---|---|---|---|
| 144 | Tris-hydroxymethyl-methyl-ammonium | C4 H12 N O3 | 1 |
| CLR | Cholesterol | C27 H46 O | 1 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 1 |
Water and common crystallization additives (NA, CL) are not listed.
Cryo-EM structure of the dopamine transporter with a novel atypical non-competitive inhibitor bound to the orthosteric site. Pedersen, C.N., Yang, F., Ita, S. et al. J Neurochem (2024) 168:2043-2055. DOI 10.1111/jnc.16179 · PubMed
Other PDB entries of the same protein (UniProt Q7K4Y6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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