Cryo-EM structure of the human SAC3D1-PCID2-SEM1 complex. Determined by electron microscopy at 3.6 Å resolution. Released 24 Jun 2026.
Explore 28WY in 3D Show helices and sheets RCSB PDB PDBe
28WY contains 44 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 | 63-71 | 9 | |
| α-helix | 77-79 | 3 | |
| β-strand | 80 | 1 | 1 |
| α-helix | 81 | 1 | |
| β-strand | 91 | 1 | 1 |
| α-helix | 93-95 | 3 | |
| α-helix | 112-114 | 3 | |
| α-helix | 118-133 | 16 | |
| α-helix | 141-159 | 19 | |
| α-helix | 166-185 | 20 | |
| α-helix | 197-217 | 21 | |
| α-helix | 225-235 | 11 | |
| α-helix | 240-247 | 8 | |
| α-helix | 251-255 | 5 | |
| α-helix | 257-271 | 15 | |
| α-helix | 274-283 | 10 | |
| α-helix | 286-311 | 26 | |
| β-strand | 317-320 | 4 | 2 |
| α-helix | 321-327 | 7 | |
| α-helix | 333-343 | 11 | |
| β-strand | 347 | 1 | 2 |
| β-strand | 352-355 | 4 | 2 |
| α-helix | 374-378 | 5 | |
| α-helix | 384-387 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-18 | 12 | |
| α-helix | 22-29 | 8 | |
| α-helix | 48-53 | 6 | |
| α-helix | 56-74 | 19 | |
| α-helix | 77-97 | 21 | |
| α-helix | 104-127 | 24 | |
| α-helix | 137-154 | 18 | |
| α-helix | 155-157 | 3 | |
| α-helix | 165-181 | 17 | |
| α-helix | 185-196 | 12 | |
| α-helix | 206-222 | 17 | |
| α-helix | 226-239 | 14 | |
| α-helix | 245-262 | 18 | |
| β-strand | 265-266 | 2 | 3 |
| α-helix | 267 | 1 | |
| α-helix | 268-274 | 7 | |
| α-helix | 277-288 | 12 | |
| α-helix | 291-300 | 10 | |
| α-helix | 302-307 | 6 | |
| α-helix | 311-333 | 23 | |
| β-strand | 337-339 | 3 | 4 |
| α-helix | 340-349 | 10 | |
| α-helix | 357-369 | 13 | |
| β-strand | 375-378 | 4 | 4 |
| β-strand | 383-386 | 4 | 4 |
| α-helix | 395-398 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-23 | 5 | |
| α-helix | 34-36 | 3 | |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 51-63 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,SAC3 domain-containing protein 1 | A | protein | 736 | Escherichia coli, Homo sapiens | A6NKF1 (AlphaFold model), P0AEX9 (AlphaFold model) |
| PCI domain-containing protein 2 | B | protein | 457 | Homo sapiens | Q5JVF3 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 70 | Homo sapiens | P60896 (AlphaFold model) |
>28WY_1 Maltose/maltodextrin-binding periplasmic protein,SAC3 domain-containing protein 1 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTSSGLEVLFQGPMPGCELPVGTCPDMCPAAERAQREREHRLHRLEVVPGCRQDP PRADPQRAVKEYSRPAAGKPRPPPSQLRPPSVLLATVRYLAGEVAESADIARAEVASFVA DRLRAVLLDLALQGAGDAEAAVVLEAALATLLTVVARLGPDAARGPADPVLLQAQVQEGF GSLRRCYARGAGPHPRQPAFQGLFLLYNLGSVEALHEVLQLPAALRACPPLRKALAVDAA FREGNAARLFRLLQTLPYLPSCAVQCHVGHARREALARFARAFSTPKGQTLPLGFMVNLL ALDGLREARDLCQAHGLPLDGEERVVFLRGRYVEEGLPPASTCKVLVESKLRGRTLEEVV MAEEEDEGTDRPGSPA
>28WY_2 PCI domain-containing protein 2 (chains B) MGKPIPNPLLGLDSTGSGKPIPNPLLGLDSTGSGKPIPNPLLGLDSTSSGLEVLFQGPMA HITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMF AAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNA DQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKI NKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHR SSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHE AFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQC ILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
>28WY_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 A6NKF1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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