11RM: Human exportin-1 conjugated with FR-027*

Cryo-EM structure of human exportin-1 conjugated with FR-027*. Determined by electron microscopy at 2.95 Å resolution. Released 29 Jul 2026.

Method
Electron microscopy
Resolution
2.95 Å
Organism
Homo sapiens
Chains
1
Atoms
7,073
Mol. weight
123.79 kDa
Ligands
A1DBJ
Released
29 Jul 2026

Explore 11RM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 55 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix164-17714
α-helix200-21314
α-helix220-23314
α-helix238-2414
α-helix246-2494
α-helix250-2545
α-helix258-2603
α-helix261-27313
α-helix280-29718
α-helix304-3107
α-helix313-33927
α-helix341-3433
α-helix344-35815
α-helix363-38321
α-helix404-42219
β-strand432-43541
β-strand439-44241
α-helix448-46720
α-helix469-48517
α-helix491-50313
α-helix510-53021
α-helix534-54815
α-helix552-5576
α-helix559-57214
α-helix578-59417
α-helix597-6004
α-helix610-6167
α-helix618-6214
α-helix627-64115
α-helix647-65711
α-helix660-67415
α-helix676-6805
α-helix682-70221
α-helix704-7063
α-helix707-73428
α-helix738-7414
α-helix743-76321
α-helix769-7713
α-helix772-7765
α-helix777-7826
α-helix785-7895
α-helix793-7953
α-helix799-81113
α-helix812-8187
α-helix819-83517
α-helix842-85817
α-helix860-8645
α-helix868-88215
α-helix887-90620
α-helix911-93222
α-helix936-9383
α-helix939-95416
α-helix970-98516
α-helix991-100313
α-helix1008-102619
α-helix1032-10343
α-helix1035-105521

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Exportin-1Aprotein1073Homo sapiensO14980 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>11RM_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

IDNameFormulaCopies
A1DBJ1-methyl-4-nitro-1H-imidazoleC4 H5 N3 O21

Primary citation

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:

Browse structure collections

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