9OGA: Human full-length XPO1 conjugated with selinexor

Cryo-EM structure of human full-length XPO1 conjugated with selinexor. Determined by electron microscopy at 3.37 Å resolution. Released 26 Nov 2025.

Method

Electron microscopy

Resolution

3.37 Å

Organism

Homo sapiens

Chains

1

Atoms

7,421

Mol. weight

124.11 kDa

Ligands

V6A

Released

26 Nov 2025

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

Secondary structure: helices and β-sheets

9OGA contains 61 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: 61 helices, 2 β-strands

Molecules and chains

>9OGA_1 Exportin-1 (chains A)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE
KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD

Ligands and cofactors

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

Related structures

Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 1W9C 2.3 Å, Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats
• 9OGD 2.49 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to human…
• 7B51 2.58 Å, Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528
• 9HFL 2.62 Å, Cryo-EM structure of the human snRNA export complex comprising CBC-PHAX-CRM1-RanGTP and…
• 5DIS 2.85 Å, Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid…
• 3GB8 2.9 Å, Crystal structure of CRM1/Snurportin-1 complex
• 9B62 2.9 Å, Human RANBP2/RAN(GTP)/RANGAP1-SUMO1/UBC9/CRM1/RAN(GTP) - composite map and model
• 9OG9 2.93 Å, Cryo-EM structure of human full-length XPO1 (unliganded)
• 11RM 2.95 Å, Cryo-EM structure of human exportin-1 conjugated with FR-027*
• 6TVO 3.2 Å, Human CRM1-RanGTP in complex with Leptomycin B
• 9OGB 3.25 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to yeast…
• 9OGE 3.28 Å, Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human…

Browse structure collections

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