apo SERT reconstituted in lipid nanodisc in KCl. Determined by electron microscopy at 3.5 Å resolution. Released 15 Dec 2021.
Explore 7LI6 in 3D Show helices and sheets RCSB PDB PDBe
7LI6 contains 36 α-helices and 33 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 | 83-86 | 4 | |
| α-helix | 89-92 | 4 | |
| α-helix | 104-111 | 8 | |
| α-helix | 118-128 | 11 | |
| α-helix | 130-142 | 13 | |
| α-helix | 150-152 | 3 | |
| α-helix | 160-189 | 30 | |
| β-strand | 209 | 1 | 1 |
| β-strand | 225 | 1 | 1 |
| α-helix | 227-231 | 5 | |
| α-helix | 232-236 | 5 | |
| β-strand | 244 | 1 | 2 |
| β-strand | 247 | 1 | 2 |
| β-strand | 251 | 1 | 3 |
| α-helix | 253-267 | 15 | |
| α-helix | 281-284 | 4 | |
| α-helix | 286-300 | 15 | |
| α-helix | 306-312 | 7 | |
| α-helix | 318-321 | 4 | |
| α-helix | 326-337 | 12 | |
| α-helix | 343-347 | 5 | |
| α-helix | 361-390 | 30 | |
| α-helix | 394-396 | 3 | |
| α-helix | 405-414 | 10 | |
| α-helix | 420-442 | 23 | |
| α-helix | 444-453 | 10 | |
| α-helix | 458-461 | 4 | |
| α-helix | 464-475 | 12 | |
| β-strand | 482 | 1 | 3 |
| α-helix | 485-489 | 5 | |
| α-helix | 491-494 | 4 | |
| α-helix | 499-510 | 12 | |
| α-helix | 511-515 | 5 | |
| α-helix | 518-529 | 12 | |
| α-helix | 535-539 | 5 | |
| α-helix | 540-544 | 5 | |
| α-helix | 545-558 | 14 | |
| β-strand | 565 | 1 | 4 |
| β-strand | 568 | 1 | 4 |
| α-helix | 573-584 | 12 | |
| α-helix | 588-599 | 12 | |
| α-helix | 604-612 | 9 | |
| α-helix | 614-616 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 22-25 | 4 | 5 |
| β-strand | 29 | 1 | 6 |
| β-strand | 37-44 | 8 | 5 |
| α-helix | 48-50 | 3 | |
| β-strand | 53-58 | 6 | 7 |
| β-strand | 64-70 | 7 | 7 |
| β-strand | 77-79 | 3 | 7 |
| β-strand | 89-90 | 2 | 5 |
| β-strand | 97-102 | 6 | 5 |
| β-strand | 112-113 | 2 | 7 |
| β-strand | 116-117 | 2 | 7 |
| β-strand | 130 | 1 | 7 |
| β-strand | 134-135 | 2 | 7 |
| β-strand | 136 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 25-26 | 2 | 8 |
| β-strand | 30-31 | 2 | 9 |
| β-strand | 43-44 | 2 | 8 |
| β-strand | 57-61 | 5 | 10 |
| β-strand | 62 | 1 | 9 |
| β-strand | 69-73 | 5 | 10 |
| β-strand | 77-78 | 2 | 10 |
| β-strand | 87-89 | 3 | 11 |
| β-strand | 96-98 | 3 | 11 |
| β-strand | 109-110 | 2 | 9 |
| β-strand | 112-114 | 3 | 10 |
| β-strand | 126-128 | 3 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium-dependent serotonin transporter | A | protein | 539 | Homo sapiens | P31645 (AlphaFold model) |
| variable domain of 15B8 antibody Fab heavy chain | B | protein | 118 | Mus musculus | |
| variable domain of 15B8 antibody Fab light chain | C | protein | 110 | Mus musculus |
>7LI6_1 Sodium-dependent serotonin transporter (chains A) RETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLPYTIMAIFGGIPLFYMELA LGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIMAWALYYLISSFTDQLPWT SCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIHRSKGLQDLGGISWQLALC IMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGATLPGAWRGVLFYLKPNWQ KLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQDALVTSVVNCMTSFVSGFV IFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPASTFFAIIFFLMLITLGLDS TFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVTLTFGGAYVVKLLEEYATG PAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRICWVAISPLFLLFIICSFLM SPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIITPGTFKERIIKSITPETP
>7LI6_2 variable domain of 15B8 antibody Fab heavy chain (chains B) QVQLQQSGPELVKLGASVRISCKASGYRFSYSWMNWVKQRPGKGLEWIGRIYPGDGDTKY SGKFKGKATLTADKSSSTVYMQLSSLTSEDSAVYFCARSAYGSEGFAMDYWGQGTSVT
>7LI6_3 variable domain of 15B8 antibody Fab light chain (chains C) DIVLTQSPASLAVSLGQRATISCRASESVDNYGISFLNWFQQKPGQPPKLLIYAASNQGS GVPARFSGSGSGTYFSLNIHPMEEDDTAVYFCQQTKGVSWTFGGGTKVEI
| ID | Name | Formula | Copies |
|---|---|---|---|
| D12 | Dodecane | C12 H26 | 3 |
| D10 | Decane | C10 H22 | 6 |
| HP6 | Heptane | C7 H16 | 9 |
| R16 | Hexadecane | C16 H34 | 1 |
| LNK | Pentane | C5 H12 | 4 |
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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