Cryo-EM structure of human serotonin transporter in complex with tesofensine. Determined by electron microscopy at 3.2 Å resolution. Released 22 Jul 2026.
Explore 9VWS in 3D Show helices and sheets RCSB PDB PDBe
9VWS contains 37 α-helices and 6 β-strands across 1 chain. 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 | 85-96 | 12 | |
| α-helix | 100-103 | 4 | |
| α-helix | 105-111 | 7 | |
| β-strand | 114 | 1 | 1 |
| α-helix | 118-124 | 7 | |
| α-helix | 125-129 | 5 | |
| α-helix | 130-143 | 14 | |
| α-helix | 151-154 | 4 | |
| α-helix | 156-158 | 3 | |
| α-helix | 160-189 | 30 | |
| α-helix | 227-231 | 5 | |
| α-helix | 232-237 | 6 | |
| α-helix | 239-241 | 3 | |
| β-strand | 251 | 1 | 2 |
| α-helix | 253-269 | 17 | |
| α-helix | 274-284 | 11 | |
| α-helix | 287-300 | 14 | |
| α-helix | 306-310 | 5 | |
| β-strand | 315 | 1 | 1 |
| α-helix | 317-321 | 5 | |
| α-helix | 323-337 | 15 | |
| α-helix | 343-349 | 7 | |
| α-helix | 357-390 | 34 | |
| α-helix | 394-396 | 3 | |
| α-helix | 403-404 | 2 | |
| α-helix | 405-409 | 5 | |
| α-helix | 410-416 | 7 | |
| α-helix | 421-453 | 33 | |
| α-helix | 463-477 | 15 | |
| α-helix | 478-481 | 4 | |
| β-strand | 482 | 1 | 2 |
| α-helix | 485-496 | 12 | |
| α-helix | 499-510 | 12 | |
| α-helix | 511-517 | 7 | |
| α-helix | 518-528 | 11 | |
| α-helix | 535-539 | 5 | |
| α-helix | 540-544 | 5 | |
| α-helix | 545-557 | 13 | |
| β-strand | 564-565 | 2 | 3 |
| β-strand | 568-569 | 2 | 3 |
| α-helix | 572-586 | 15 | |
| α-helix | 588-599 | 12 | |
| α-helix | 604-612 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium-dependent serotonin transporter | A | protein | 630 | Homo sapiens | P31645 (AlphaFold model) |
>9VWS_1 Sodium-dependent serotonin transporter (chains A) METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTR HSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLP YTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIM AWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIH RSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGA TLPGAWRGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQD ALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPAS TFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVT LTFGGAYVVKLLEEYATGPAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRIC WVAISPLFLLFIICSFLMSPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIIT PGTFKERIIKSITPETPTEIPCGDIRLNAV
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1EA1 | (1~{R},2~{R},3~{S},5~{S})-3-(3,4-dichlorophenyl)-2-(ethoxymethyl)-8-methyl-8-az… | C17 H23 Cl2 N O | 1 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 1 |
Water and common crystallization additives (CL, NA) are not listed.
Structural basis for pharmacotherapeutic action of triple reuptake inhibitors. Li, Y., Meng, Y., Li, N. et al. Nat Commun (2025) 17:61-61. DOI 10.1038/s41467-025-66670-3 · PubMed
Other PDB entries of the same protein (UniProt P31645 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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