9OGC: Human exportin-1 conjugated with KPT-185 and

Cryo-EM structure of human exportin-1 conjugated with KPT-185 and bound to human ASB8-ELOB/C. Determined by electron microscopy at 3.37 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 3.37 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,758
Mol. weight: 178.01 kDa
Ligands: K85
Released: 26 Nov 2025

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

Secondary structure: helices and β-sheets

9OGC contains 78 α-helices and 16 β-strands across 4 chains. 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: 54 helices, 0 β-strands

Element	Residues	Length
α-helix	219-232	14
α-helix	264-271	8
α-helix	272-274	3
α-helix	280-297	18
α-helix	304-310	7
α-helix	313-339	27
α-helix	341-343	3
α-helix	344-357	14
α-helix	363-381	19
α-helix	406-408	3
α-helix	410-422	13
α-helix	449-467	19
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	596-600	5
α-helix	602-603	2
α-helix	610-616	7
α-helix	618-622	5
α-helix	627-641	15
α-helix	647-657	11
α-helix	659-674	16
α-helix	676-679	4
α-helix	682-702	21
α-helix	704-706	3
α-helix	707-735	29
α-helix	738-741	4
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	798-810	13
α-helix	814-817	4
α-helix	819-822	4
α-helix	823-827	5
α-helix	828-835	8
α-helix	842-858	17
α-helix	860-865	6
α-helix	868-881	14
α-helix	887-904	18
α-helix	908-914	7
α-helix	915-919	5
α-helix	920-932	13
α-helix	939-954	16
α-helix	970-985	16
α-helix	991-1003	13
α-helix	1004-1006	3
α-helix	1008-1026	19
α-helix	1031-1055	25

Chain B: 15 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	56-62	7
α-helix	66-74	9
α-helix	89-96	8
α-helix	98-105	8
α-helix	121-128	8
α-helix	131-140	10
α-helix	154-161	8
α-helix	165-172	8
α-helix	187-196	10
α-helix	202-215	14
β-strand	222	1	1
β-strand	225	1	1
α-helix	228-231	4
α-helix	234-245	12
α-helix	250-262	13
α-helix	267-272	6
α-helix	278-284	7

Chain E: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	19-22	4	2
β-strand	28-31	4	2
α-helix	33-36	4
α-helix	40-45	6
β-strand	59-61	3	2
α-helix	67-83	17
α-helix	91-93	3
α-helix	97-109	13

Chain F: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	2
β-strand	10	1	3
β-strand	12-19	8	2
β-strand	23	1	4
α-helix	24-35	12
α-helix	39-41	3
β-strand	42-46	5	2
β-strand	49-50	2	2
β-strand	56	1	4
β-strand	73-79	7	2
β-strand	80-81	2	5
β-strand	84-85	2	5
α-helix	86-87	2
β-strand	90	1	3
α-helix	92-100	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Exportin-1	A	protein	1073	Homo sapiens	O14980 (AlphaFold model)
Ankyrin repeat and SOCS box protein 8	B	protein	274	Homo sapiens	Q9H765 (AlphaFold model)
Elongin-C	E	protein	97	Homo sapiens	Q15369 (AlphaFold model)
Elongin-B	F	protein	118	Homo sapiens	Q15370 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9OGC_1 Exportin-1 (chains A)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE
KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD

Sequence of entity 2 (B), FASTA

>9OGC_2 Ankyrin repeat and SOCS box protein 8 (chains B)
GSSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLE
KGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECV
RALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVAL
LVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLA
RYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE

Sequence of entity 3 (E), FASTA

>9OGC_3 Elongin-C (chains E)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC

Sequence of entity 4 (F), FASTA

>9OGC_4 Elongin-B (chains F)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ

Ligands and cofactors

ID	Name	Formula	Copies
K85	propan-2-yl 3-{3-[3-methoxy-5-(trifluoromethyl)phenyl]-1H-1,2,4-triazol-1-yl}pr…	C16 H18 F3 N3 O3	1

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:

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…

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