Cryo-EM structure of the human UAP56-RNA - LENG8-PCID2-SEM1 complex. Determined by electron microscopy at 6.2 Å resolution. Released 24 Jun 2026.
Explore 28XB in 3D Show helices and sheets RCSB PDB PDBe
28XB contains 65 α-helices and 24 β-strands across 4 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 | 567-569 | 3 | |
| α-helix | 574-575 | 2 | |
| α-helix | 576-592 | 17 | |
| α-helix | 596-613 | 18 | |
| α-helix | 618-634 | 17 | |
| α-helix | 637-653 | 17 | |
| α-helix | 659-673 | 15 | |
| α-helix | 676-685 | 10 | |
| α-helix | 688-692 | 5 | |
| α-helix | 694-698 | 5 | |
| α-helix | 700-708 | 9 | |
| α-helix | 711-720 | 10 | |
| α-helix | 725-747 | 23 | |
| β-strand | 748 | 1 | 1 |
| β-strand | 751-753 | 3 | 2 |
| α-helix | 754-760 | 7 | |
| α-helix | 766-776 | 11 | |
| β-strand | 780-781 | 2 | 2 |
| α-helix | 783-785 | 3 | |
| β-strand | 787-789 | 3 | 2 |
| α-helix | 790-799 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-19 | 12 | |
| α-helix | 22-29 | 8 | |
| α-helix | 49-53 | 5 | |
| α-helix | 58-73 | 16 | |
| α-helix | 77-97 | 21 | |
| α-helix | 101-128 | 28 | |
| α-helix | 136-153 | 18 | |
| α-helix | 164-166 | 3 | |
| α-helix | 168-182 | 15 | |
| α-helix | 185-197 | 13 | |
| α-helix | 199-201 | 3 | |
| α-helix | 206-222 | 17 | |
| α-helix | 226-239 | 14 | |
| α-helix | 245-261 | 17 | |
| β-strand | 265-266 | 2 | 3 |
| α-helix | 267 | 1 | |
| α-helix | 268-273 | 6 | |
| α-helix | 277-288 | 12 | |
| α-helix | 291-300 | 10 | |
| α-helix | 302-308 | 7 | |
| α-helix | 310-333 | 24 | |
| β-strand | 337-339 | 3 | 1 |
| α-helix | 340-349 | 10 | |
| α-helix | 357-369 | 13 | |
| β-strand | 377-378 | 2 | 1 |
| α-helix | 379-381 | 3 | |
| β-strand | 383-385 | 3 | 1 |
| α-helix | 395-398 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-38 | 5 | |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 41-43 | 3 | |
| α-helix | 51-63 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 47-50 | 4 | |
| α-helix | 54-63 | 10 | |
| α-helix | 70-80 | 11 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 95-106 | 12 | |
| β-strand | 116-119 | 4 | 5 |
| β-strand | 120 | 1 | 4 |
| α-helix | 123-136 | 14 | |
| α-helix | 137-139 | 3 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-163 | 10 | |
| β-strand | 168-171 | 4 | 5 |
| α-helix | 173-181 | 9 | |
| α-helix | 187-189 | 3 | |
| β-strand | 192-196 | 5 | 4 |
| α-helix | 198-203 | 6 | |
| α-helix | 205-217 | 13 | |
| β-strand | 223-227 | 5 | 4 |
| α-helix | 235-242 | 8 | |
| α-helix | 246 | 1 | |
| β-strand | 247-250 | 4 | 4 |
| β-strand | 262-268 | 7 | 6 |
| α-helix | 271-284 | 14 | |
| β-strand | 290-293 | 4 | 6 |
| α-helix | 297-309 | 13 | |
| β-strand | 314-316 | 3 | 6 |
| α-helix | 323-334 | 12 | |
| β-strand | 340-343 | 4 | 6 |
| α-helix | 345-348 | 4 | |
| β-strand | 359-361 | 3 | 6 |
| α-helix | 368-376 | 9 | |
| β-strand | 385-391 | 7 | 6 |
| α-helix | 394-407 | 14 | |
| β-strand | 412-413 | 2 | 6 |
| α-helix | 414 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Leukocyte receptor cluster member 8,Leukocyte… | A | protein | 688 | Escherichia coli, Homo sapiens | Q96PV6 (AlphaFold model) |
| PCI domain-containing protein 2 | B | protein | 456 | Homo sapiens | Q5JVF3 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 49 | Homo sapiens | P60896 (AlphaFold model) |
| Spliceosome RNA helicase DDX39B | H | protein | 428 | Homo sapiens | Q13838 (AlphaFold model) |
| RNA (5'-r(p*up*up*up*up*up*u)-3') | 1 | RNA | 6 | Homo sapiens |
>28XB_1 Maltose/maltodextrin-binding periplasmic protein,Leukocyte receptor cluster member 8,Leukocyte receptor cluster member 8,Leukocyte receptor cluster member 8,Leukocyte receptor cluster member 8 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDE ALKDAQTSSGLEVLFQGPSRKKMAALECEDPERELKKQKRAARFQHGHSRRLRLEPLVLQ MSSLESSGADPDWQELQIVGTCPDITKHYLRLTCAPDPSTVRPVAVLKKSLCMVKCHWKE KQDYAFACEQMKSIRQDLTVQGIRTEFTVEVYETHARIALEKGDHEEFNQCQTQLKSLYA ENLPGNVGEFTAYRILYYIFTKNSGDITTELAYLTRELKADPCVAHALALRTAWALGNYH RFFRLYCHAPCMSGYLVDKFADRERKVALKAMIKTFRPALPVSYLQAELAFEGEAACRAF LEPLGLAYTGPDNSSIDCRLSLAQLSAF
>28XB_2 PCI domain-containing protein 2 (chains B) GKPIPNPLLGLDSTGSGKPIPNPLLGLDSTGSGKPIPNPLLGLDSTSSGLEVLFQGPMAH ITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDEMFA AHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFANNAD QQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYFKIN KLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHCHRS SQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAKHEA FFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEVQCI LANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
>28XB_3 26S proteasome complex subunit SEM1 (chains C) FPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAELEKHGYKMETS
>28XB_4 Spliceosome RNA helicase DDX39B (chains H) MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAI VDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMC HTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALA RNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCR KFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRC IALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAF NYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDI SSYIEQTR
>28XB_5 RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') (chains 1) UUUUUU
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 Q96PV6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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