5-HT bound serotonin transporter reconstituted in lipid nanodisc in NaCl in occluded conformation. Determined by electron microscopy at 3.5 Å resolution. Released 15 Dec 2021.
Explore 7MGW in 3D Show helices and sheets RCSB PDB PDBe
7MGW contains 35 α-helices and 31 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 | 85-96 | 12 | |
| α-helix | 99-112 | 14 | |
| α-helix | 115-117 | 3 | |
| α-helix | 119-121 | 3 | |
| α-helix | 122-143 | 22 | |
| α-helix | 149-151 | 3 | |
| α-helix | 156-158 | 3 | |
| α-helix | 161-189 | 29 | |
| β-strand | 209 | 1 | 1 |
| β-strand | 225 | 1 | 1 |
| α-helix | 227-234 | 8 | |
| α-helix | 239-241 | 3 | |
| α-helix | 253-272 | 20 | |
| α-helix | 274-283 | 10 | |
| α-helix | 286-299 | 14 | |
| α-helix | 307-312 | 6 | |
| α-helix | 326-337 | 12 | |
| α-helix | 343-348 | 6 | |
| α-helix | 357-390 | 34 | |
| α-helix | 394-396 | 3 | |
| α-helix | 404-416 | 13 | |
| α-helix | 423-453 | 31 | |
| α-helix | 455-460 | 6 | |
| α-helix | 462-481 | 20 | |
| α-helix | 486-495 | 10 | |
| α-helix | 499-510 | 12 | |
| α-helix | 511-515 | 5 | |
| α-helix | 518-529 | 12 | |
| α-helix | 537-539 | 3 | |
| α-helix | 540-544 | 5 | |
| α-helix | 545-558 | 14 | |
| β-strand | 564 | 1 | 2 |
| β-strand | 569 | 1 | 2 |
| α-helix | 570-571 | 2 | |
| α-helix | 572-584 | 13 | |
| α-helix | 588-599 | 12 | |
| α-helix | 604-611 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24-25 | 2 | 3 |
| β-strand | 29 | 1 | 4 |
| β-strand | 38-42 | 5 | 3 |
| β-strand | 53-58 | 6 | 5 |
| β-strand | 64-71 | 8 | 5 |
| β-strand | 76-79 | 4 | 5 |
| β-strand | 87-92 | 6 | 3 |
| β-strand | 97-102 | 6 | 3 |
| β-strand | 112-113 | 2 | 5 |
| β-strand | 116-117 | 2 | 5 |
| β-strand | 129 | 1 | 5 |
| β-strand | 134-135 | 2 | 5 |
| β-strand | 136 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-27 | 3 | 6 |
| β-strand | 30-31 | 2 | 7 |
| α-helix | 33-34 | 2 | |
| β-strand | 39-44 | 6 | 6 |
| β-strand | 50-51 | 2 | 8 |
| β-strand | 54-55 | 2 | 8 |
| β-strand | 58-62 | 5 | 9 |
| α-helix | 67-68 | 2 | |
| β-strand | 69-73 | 5 | 9 |
| β-strand | 77-78 | 2 | 9 |
| β-strand | 86 | 1 | 6 |
| β-strand | 89-91 | 3 | 6 |
| β-strand | 94-99 | 6 | 6 |
| β-strand | 109-114 | 6 | 9 |
| β-strand | 121-122 | 2 | 9 |
| β-strand | 127-128 | 2 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium-dependent serotonin transporter | A | protein | 537 | Homo sapiens | P31645 (AlphaFold model) |
| variable domain of 15B8 antibody Fab heavy chain | B | protein | 118 | Mus musculus | |
| variable domain of 15B8 antiboty Fab light chain | C | protein | 110 | Mus musculus |
>7MGW_1 Sodium-dependent serotonin transporter (chains A) RETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELA LGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWT SCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALC IMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQ KLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFV IFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDS TFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVTLTFGGAYVVKLLEEYATG PAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLM SPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIITPGTFKERIIKSITPE
>7MGW_2 variable domain of 15B8 antibody Fab heavy chain (chains B) QVQLQQSGPELVKLGASVRISCKASGYRFSYSWMNWVKQRPGKGLEWIGRIYPGDGDTKY SGKFKGKATLTADKSSSTVYMQLSSLTSEDSAVYFCARSAYGSEGFAMDYWGQGTSVT
>7MGW_3 variable domain of 15B8 antiboty Fab light chain (chains C) DIVLTQSPASLAVSLGQRATISCRASESVDNYGISFLNWFQQKPGQPPKLLIYAASNQGS GVPARFSGSGSGTYFSLNIHPMEEDDTAVYFCQQTKGVSWTFGGGTKVEI
| ID | Name | Formula | Copies |
|---|---|---|---|
| D10 | Decane | C10 H22 | 1 |
| HP6 | Heptane | C7 H16 | 6 |
| LNK | Pentane | C5 H12 | 1 |
| D12 | Dodecane | C12 H26 | 4 |
| CLR | Cholesterol | C27 H46 O | 1 |
| SRO | Serotonin | C10 H12 N2 O | 2 |
Water and common crystallization additives (CL) are not listed.
Illumination of serotonin transporter mechanism and role of the allosteric site. Yang, D., Gouaux, E. Sci Adv (2021) 7:eabl3857-eabl3857. DOI 10.1126/sciadv.abl3857 · 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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