Cryo-EM structure of human full-length XPO1 (unliganded). Determined by electron microscopy at 2.93 Å resolution. Released 26 Nov 2025.
Explore 9OG9 in 3D Show helices and sheets RCSB PDB PDBe
9OG9 contains 60 α-helices and 2 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 | 128-139 | 12 | |
| α-helix | 153-155 | 3 | |
| α-helix | 164-177 | 14 | |
| α-helix | 199-202 | 4 | |
| α-helix | 203-215 | 13 | |
| α-helix | 219-232 | 14 | |
| α-helix | 238-243 | 6 | |
| α-helix | 246-253 | 8 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-272 | 12 | |
| α-helix | 280-297 | 18 | |
| α-helix | 304-310 | 7 | |
| α-helix | 313-339 | 27 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-358 | 15 | |
| α-helix | 363-383 | 21 | |
| α-helix | 404-422 | 19 | |
| α-helix | 424-427 | 4 | |
| β-strand | 432-435 | 4 | 1 |
| β-strand | 439-442 | 4 | 1 |
| α-helix | 448-467 | 20 | |
| α-helix | 469-485 | 17 | |
| α-helix | 491-502 | 12 | |
| α-helix | 510-530 | 21 | |
| α-helix | 534-549 | 16 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-572 | 14 | |
| α-helix | 578-594 | 17 | |
| α-helix | 596-598 | 3 | |
| α-helix | 610-616 | 7 | |
| α-helix | 618-621 | 4 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-674 | 16 | |
| α-helix | 676-680 | 5 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-735 | 29 | |
| α-helix | 737-741 | 5 | |
| α-helix | 743-765 | 23 | |
| α-helix | 769-771 | 3 | |
| α-helix | 772-776 | 5 | |
| α-helix | 777-790 | 14 | |
| α-helix | 793-795 | 3 | |
| α-helix | 799-811 | 13 | |
| α-helix | 812-815 | 4 | |
| α-helix | 819-822 | 4 | |
| α-helix | 823-827 | 5 | |
| α-helix | 828-834 | 7 | |
| α-helix | 838-840 | 3 | |
| α-helix | 842-858 | 17 | |
| α-helix | 860-864 | 5 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-904 | 18 | |
| α-helix | 908-932 | 25 | |
| α-helix | 936-938 | 3 | |
| α-helix | 939-954 | 16 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1026 | 19 | |
| α-helix | 1031-1034 | 4 | |
| α-helix | 1035-1054 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exportin-1 | A | protein | 1073 | Homo sapiens | O14980 (AlphaFold model) |
>9OG9_1 Exportin-1 (chains A) GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
SINE compounds activate exportin 1 degradation through an allosteric mechanism. Wing, C.E., Fung, H.Y.J., Kwanten, B. et al. Nat Chem Biol (2025) 21:2002-2013. DOI 10.1038/s41589-025-02058-0 · PubMed
Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9OG9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.