Cryo-EM structure of human exportin-1 conjugated with FR-027*. Determined by electron microscopy at 2.95 Å resolution. Released 29 Jul 2026.
Explore 11RM in 3D Show helices and sheets RCSB PDB PDBe
11RM contains 55 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 | 164-177 | 14 | |
| α-helix | 200-213 | 14 | |
| α-helix | 220-233 | 14 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-254 | 5 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-273 | 13 | |
| 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 | |
| β-strand | 432-435 | 4 | 1 |
| β-strand | 439-442 | 4 | 1 |
| α-helix | 448-467 | 20 | |
| α-helix | 469-485 | 17 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 534-548 | 15 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-572 | 14 | |
| α-helix | 578-594 | 17 | |
| α-helix | 597-600 | 4 | |
| α-helix | 610-616 | 7 | |
| α-helix | 618-621 | 4 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 660-674 | 15 | |
| α-helix | 676-680 | 5 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-734 | 28 | |
| α-helix | 738-741 | 4 | |
| α-helix | 743-763 | 21 | |
| α-helix | 769-771 | 3 | |
| α-helix | 772-776 | 5 | |
| α-helix | 777-782 | 6 | |
| α-helix | 785-789 | 5 | |
| α-helix | 793-795 | 3 | |
| α-helix | 799-811 | 13 | |
| α-helix | 812-818 | 7 | |
| α-helix | 819-835 | 17 | |
| α-helix | 842-858 | 17 | |
| α-helix | 860-864 | 5 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 911-932 | 22 | |
| 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 | 1032-1034 | 3 | |
| α-helix | 1035-1055 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exportin-1 | A | protein | 1073 | Homo sapiens | O14980 (AlphaFold model) |
>11RM_1 Exportin-1 (chains A) GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1DBJ | 1-methyl-4-nitro-1H-imidazole | C4 H5 N3 O2 | 1 |
Preclinical characterization of a reversible XPO1 inhibitor for cancer therapy. Van Hauwenhuyse, J., Reniers, F., Persoons, L. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75741-y · PubMed
Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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