Cryo-EM structure of the human LENG8-PCID2-SEM1 complex. Determined by electron microscopy at 3.5 Å resolution. Released 24 Jun 2026.
Explore 28WZ in 3D Show helices and sheets RCSB PDB PDBe
28WZ contains 37 α-helices and 10 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 | 576-592 | 17 | |
| α-helix | 596-612 | 17 | |
| α-helix | 618-632 | 15 | |
| α-helix | 637-653 | 17 | |
| α-helix | 659-673 | 15 | |
| α-helix | 676-685 | 10 | |
| α-helix | 688-692 | 5 | |
| α-helix | 695-708 | 14 | |
| α-helix | 711-720 | 10 | |
| α-helix | 725-747 | 23 | |
| β-strand | 752-753 | 2 | 1 |
| α-helix | 754-761 | 8 | |
| α-helix | 766-776 | 11 | |
| α-helix | 778-779 | 2 | |
| β-strand | 780 | 1 | 1 |
| β-strand | 787-788 | 2 | 1 |
| α-helix | 790-796 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-30 | 23 | |
| α-helix | 58-74 | 17 | |
| α-helix | 77-97 | 21 | |
| α-helix | 105-129 | 25 | |
| α-helix | 136-154 | 19 | |
| α-helix | 155-157 | 3 | |
| α-helix | 164-182 | 19 | |
| α-helix | 185-187 | 3 | |
| α-helix | 188-197 | 10 | |
| α-helix | 206-223 | 18 | |
| α-helix | 226-239 | 14 | |
| β-strand | 241 | 1 | 2 |
| α-helix | 245-262 | 18 | |
| α-helix | 264 | 1 | |
| β-strand | 265-266 | 2 | 3 |
| α-helix | 267 | 1 | |
| α-helix | 268-274 | 7 | |
| α-helix | 277-288 | 12 | |
| α-helix | 291-305 | 15 | |
| α-helix | 311-333 | 23 | |
| β-strand | 338-339 | 2 | 4 |
| α-helix | 340-350 | 11 | |
| α-helix | 357-370 | 14 | |
| β-strand | 376-378 | 3 | 4 |
| β-strand | 383-385 | 3 | 4 |
| α-helix | 395-397 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| β-strand | 32 | 1 | 2 |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 51-61 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Leukocyte receptor cluster member 8 | A | protein | 687 | Escherichia coli, Homo sapiens | P0AEX9 (AlphaFold model), Q96PV6 (AlphaFold model) |
| PCI domain-containing protein 2 | B | protein | 456 | Homo sapiens | Q5JVF3 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 70 | Homo sapiens | P60896 (AlphaFold model) |
>28WZ_1 Maltose/maltodextrin-binding periplasmic protein,Leukocyte receptor cluster member 8 (chains A) KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA LKDAQTSSGLEVLFQGPSRKKMAALECEDPERELKKQKRAARFQHGHSRRLRLEPLVLQM SSLESSGADPDWQELQIVGTCPDITKHYLRLTCAPDPSTVRPVAVLKKSLCMVKCHWKEK QDYAFACEQMKSIRQDLTVQGIRTEFTVEVYETHARIALEKGDHEEFNQCQTQLKSLYAE NLPGNVGEFTAYRILYYIFTKNSGDITTELAYLTRELKADPCVAHALALRTAWALGNYHR FFRLYCHAPCMSGYLVDKFADRERKVALKAMIKTFRPALPVSYLQAELAFEGEAACRAFL EPLGLAYTGPDNSSIDCRLSLAQLSAF
>28WZ_2 PCI domain-containing protein 2 (chains B) GKPIPNPLLGLDSTGSGKPIPNPLLGLDSTGSGKPIPNPLLGLDSTSSGLEVLFQGPMAH ITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFA AHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNAD QQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKIN KLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRS SQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEA FFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCI LANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
>28WZ_3 26S proteasome complex subunit SEM1 (chains C) MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAEL EKHGYKMETS
Molecular basis of polyadenylated RNA fate determination in the nucleus. Bugai, A., Hohmann, U., Lorenzo, A. et al. Nature (2026) 655:1070-1078. DOI 10.1038/s41586-026-10650-0 · PubMed
Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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