cryoEM structure of human Nup155 (residues 19-981). Determined by electron microscopy at 3.0 Å resolution. Released 8 Jun 2022.
Explore 7R1Y in 3D Show helices and sheets RCSB PDB PDBe
7R1Y contains 31 α-helices and 33 β-strands across 1 chain. 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 | 20-36 | 17 | |
| α-helix | 43-46 | 4 | |
| β-strand | 56-58 | 3 | 1 |
| β-strand | 85-88 | 4 | 2 |
| α-helix | 89-90 | 2 | |
| α-helix | 91-98 | 8 | |
| β-strand | 106-107 | 2 | 3 |
| β-strand | 115-117 | 3 | 3 |
| β-strand | 124-127 | 4 | 3 |
| β-strand | 132-135 | 4 | 3 |
| β-strand | 146-150 | 5 | 4 |
| α-helix | 151-153 | 3 | |
| β-strand | 164-168 | 5 | 4 |
| β-strand | 172-177 | 6 | 4 |
| β-strand | 207-209 | 3 | 4 |
| β-strand | 215-220 | 6 | 5 |
| β-strand | 226-230 | 5 | 5 |
| β-strand | 235-239 | 5 | 5 |
| β-strand | 252-255 | 4 | 5 |
| β-strand | 265-271 | 7 | 6 |
| β-strand | 276-281 | 6 | 6 |
| β-strand | 286-290 | 5 | 6 |
| β-strand | 299-304 | 6 | 6 |
| α-helix | 306-317 | 12 | |
| α-helix | 322-325 | 4 | |
| β-strand | 328-333 | 6 | 1 |
| β-strand | 344-348 | 5 | 1 |
| β-strand | 352-357 | 6 | 1 |
| α-helix | 366-368 | 3 | |
| β-strand | 372-377 | 6 | 1 |
| α-helix | 380-382 | 3 | |
| α-helix | 389-391 | 3 | |
| β-strand | 394-400 | 7 | 7 |
| β-strand | 403-408 | 6 | 7 |
| β-strand | 414-421 | 8 | 7 |
| β-strand | 434-441 | 8 | 7 |
| β-strand | 446-449 | 4 | 2 |
| α-helix | 482-484 | 3 | |
| β-strand | 485-489 | 5 | 2 |
| β-strand | 493-498 | 6 | 2 |
| α-helix | 499-501 | 3 | |
| α-helix | 502-512 | 11 | |
| α-helix | 520-527 | 8 | |
| α-helix | 530-541 | 12 | |
| α-helix | 549-561 | 13 | |
| α-helix | 647-660 | 14 | |
| α-helix | 661-663 | 3 | |
| β-strand | 667 | 1 | 8 |
| β-strand | 670-671 | 2 | 9 |
| β-strand | 684-685 | 2 | 9 |
| α-helix | 690-709 | 20 | |
| α-helix | 761-786 | 26 | |
| α-helix | 789-794 | 6 | |
| α-helix | 798-805 | 8 | |
| β-strand | 808 | 1 | 8 |
| α-helix | 809-810 | 2 | |
| α-helix | 811-815 | 5 | |
| α-helix | 819-833 | 15 | |
| α-helix | 839-848 | 10 | |
| α-helix | 855-869 | 15 | |
| α-helix | 876-891 | 16 | |
| α-helix | 899-908 | 10 | |
| α-helix | 912-926 | 15 | |
| α-helix | 951-966 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear pore complex protein Nup155 | A | protein | 1388 | Homo sapiens | O75694 (AlphaFold model) |
>7R1Y_1 Nuclear pore complex protein Nup155 (chains A) GPPSSLLGAAMPASTSAAALQEALENAGRLIDRQLQEDRMYPDLSELLMVSAPNNPTVSG MSDMDYPLQGPGLLSVPNLPEISSIRRVPLPPELVEQFGHMQCNCMMGVFPPISRAWLTI DSDIFMWNYEDGGDLAYFDGLSETILAVGLVKPKAGIFQPHVRHLLVLATPVDIVILGLS YANLQTGSGVLNDSLSGGMQLLPDPLYSLPTDNTYLLTITSTDNGRIFLAGKDGCLYEVA YQAEAGWFSQRCRKINHSKSSEDDPILQIAIDNSRNILYTRSEKGVIQVYDLGQDGQGMS RVASVSQNAIVSAAGNIARTIDRSVFKPIVQIAVIENSESLDCQLLAVTHAGVRLYFSTC PFRQPLARPNTLTLVHVRLPPGFSASSTVEKPSKVHRALYSKGILLMAASENEDNDILWC VNHDTFPFQKPMMETQMTAGVDGHSWALSAIDELKVDKIITPLNKDHIPITDSPVVVQQH MLPPKKFVLLSAQGSLMFHKLRPVDQLRHLLVSNVGGDGEEIERFFKLHQEDQACATCLI LACSTAACDREVSAWATRAFFRYGGEAQMRFPTTLPPPSNVGPILGSPVYSSSPVPSGSP YPNPSFLGTPSHGIQPPAMSTPVCALGNPATQATNMSCVTGPEIVYSGKHNGICIYFSRI MGNIWDASLVVERIFKSGNREITAIESSVPCQLLESVLQELKGLQEFLDRNSQFAGGPLG NPNTTAKVQQRLIGFMRPENGNPQQMQQELQRKFHEAQLSEKISLQAIQQLVRKSYQALA LWKLLCEHQFTIIVAELQKELQEQLKITTFKDLVIRDKELTGALIASLINCYIRDNAAVD GISLHLQDICPLLYSTDDAICSKANELLQRSRQVQNKTEKERMLRESLKEYQKISNQVDL SNVCAQYRQVRFYEGVVELSLTAAEKKDPQGLGLHFYKHGEPEEDIVGLQAFQERLNSYK CITDTLQELVNQSKAAPQSPSVPKKPGPPVLSSDPNMLSNEEAGHHFEQMLKLSQRSKDE LFSIALYNWLIQVDLADKLLQVASPFLEPHLVRMAKVDQNRVRYMDLLWRYYEKNRSFSN AARVLSRLADMHSTEISLQQRLEYIARAILSAKSSTAISSIAADGEFLHELEEKMEVARI QLQIQETLQRQYSHHSSVQDAVSQLDSELMDITKLYGEFADPFKLAECKLAIIHCAGYSD PILVQTLWQDIIEKELSDSVTLSSSDRMHALSLKIVLLGKIYAGTPRFFPLDFIVQFLEQ QVCTLNWDVGFVIQTMNEIGVPLPRLLEVYDQLFKSRDPFWNRMKKPLHLLDCIHVLLIR YVENPSQVLNCERRRFTNLCLDAVCGYLVELQSMSSSVAVQAITGNFKSLQAKLERLHSA WSHPQFEK
AI-based structure prediction empowers integrative structural analysis of human nuclear pores. Mosalaganti, S., Obarska-Kosinska, A., Siggel, M. et al. Science (2022) 376:eabm9506-eabm9506. DOI 10.1126/science.abm9506 · PubMed
Other PDB entries of the same protein (UniProt O75694 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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