9OG9: Human full-length XPO1

Cryo-EM structure of human full-length XPO1 (unliganded). Determined by electron microscopy at 2.93 Å resolution. Released 26 Nov 2025.

Method
Electron microscopy
Resolution
2.93 Å
Organism
Homo sapiens
Chains
1
Atoms
7,321
Mol. weight
123.66 kDa
Released
26 Nov 2025

Explore 9OG9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 60 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix128-13912
α-helix153-1553
α-helix164-17714
α-helix199-2024
α-helix203-21513
α-helix219-23214
α-helix238-2436
α-helix246-2538
α-helix258-2603
α-helix261-27212
α-helix280-29718
α-helix304-3107
α-helix313-33927
α-helix341-3433
α-helix344-35815
α-helix363-38321
α-helix404-42219
α-helix424-4274
β-strand432-43541
β-strand439-44241
α-helix448-46720
α-helix469-48517
α-helix491-50212
α-helix510-53021
α-helix534-54916
α-helix552-5576
α-helix559-57214
α-helix578-59417
α-helix596-5983
α-helix610-6167
α-helix618-6214
α-helix627-64115
α-helix647-65711
α-helix659-67416
α-helix676-6805
α-helix682-70221
α-helix704-7063
α-helix707-73529
α-helix737-7415
α-helix743-76523
α-helix769-7713
α-helix772-7765
α-helix777-79014
α-helix793-7953
α-helix799-81113
α-helix812-8154
α-helix819-8224
α-helix823-8275
α-helix828-8347
α-helix838-8403
α-helix842-85817
α-helix860-8645
α-helix868-88215
α-helix887-90418
α-helix908-93225
α-helix936-9383
α-helix939-95416
α-helix970-98516
α-helix991-100313
α-helix1008-102619
α-helix1031-10344
α-helix1035-105420

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Exportin-1Aprotein1073Homo sapiensO14980 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9OG9_1 Exportin-1 (chains A)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE
KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD

Primary citation

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:

Browse structure collections

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