9OGB: Human exportin-1 conjugated with selinexor and

Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to yeast RAN-GTP and human ASB8-ELOB/C. Determined by electron microscopy at 3.25 Å resolution. Released 26 Nov 2025.

Method: Electron microscopy
Resolution: 3.25 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae
Chains: 5
Atoms: 13,129
Mol. weight: 199.21 kDa
Ligands: GTP, MG, V6A
Released: 26 Nov 2025

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

Secondary structure: helices and β-sheets

9OGB contains 95 α-helices and 23 β-strands across 5 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: 59 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-13	4
α-helix	14-17	4
α-helix	25-36	12
α-helix	40-55	16
α-helix	59-69	11
α-helix	73-89	17
α-helix	91-93	3
α-helix	96-114	19
α-helix	124-145	22
α-helix	149-159	11
α-helix	161-179	19
α-helix	188-214	27
α-helix	219-232	14
α-helix	238-242	5
α-helix	246-254	9
α-helix	258-273	16
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	430-435	6	1
β-strand	439-444	6	1
α-helix	449-484	36
α-helix	491-503	13
α-helix	510-530	21
α-helix	534-549	16
α-helix	552-555	4
α-helix	559-572	14
α-helix	580-599	20
α-helix	610-621	12
α-helix	627-642	16
α-helix	647-674	28
α-helix	676-680	5
α-helix	682-702	21
α-helix	704-706	3
α-helix	707-711	5
α-helix	714-735	22
α-helix	737-741	5
α-helix	743-765	23
α-helix	769-775	7
α-helix	777-780	4
α-helix	781-785	5
α-helix	786-790	5
α-helix	793-795	3
α-helix	799-811	13
α-helix	812-818	7
α-helix	819-834	16
α-helix	842-858	17
α-helix	860-865	6
α-helix	868-882	15
α-helix	887-904	18
α-helix	908-930	23
α-helix	933-938	6
α-helix	939-955	17
α-helix	970-985	16
α-helix	991-1003	13
α-helix	1008-1021	14
α-helix	1035-1050	16

Chain B: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	13-18	6	2
α-helix	25-34	10
β-strand	47-56	10	2
β-strand	59-68	10	2
α-helix	78-82	5
β-strand	87-93	7	2
α-helix	97-101	5
α-helix	103-111	9
β-strand	119-124	6	2
α-helix	140-143	4
β-strand	147-150	4	2
α-helix	161-167	7
α-helix	168-172	5
β-strand	178	1	2

Chain C: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	56-63	8
α-helix	66-72	7
α-helix	73-78	6
α-helix	89-96	8
α-helix	98-106	9
α-helix	121-127	7
α-helix	131-139	9
α-helix	154-161	8
α-helix	164-172	9
α-helix	187-196	10
α-helix	202-215	14
α-helix	222-224	3
α-helix	228-231	4
α-helix	234-245	12
α-helix	250-262	13
α-helix	267-271	5
α-helix	278-284	7

Chain E: 6 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	19-22	4	3
β-strand	28-31	4	3
α-helix	33-36	4
α-helix	40-45	6
β-strand	59-61	3	3
α-helix	67-83	17
α-helix	89-92	4
α-helix	97-99	3
α-helix	100-110	11

Chain F: 6 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	3
β-strand	10	1	4
β-strand	12-19	8	3
β-strand	23	1	5
α-helix	24-34	11
β-strand	43-46	4	3
β-strand	49-51	3	3
α-helix	52	1
β-strand	56	1	5
β-strand	73-78	6	3
β-strand	80	1	6
β-strand	85	1	6
α-helix	86-88	3
β-strand	90	1	4
α-helix	91-96	6
α-helix	98-100	3
α-helix	101-103	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Exportin-1	A	protein	1073	Homo sapiens	O14980 (AlphaFold model)
GTP-binding nuclear protein GSP1/CNR1	B	protein	181	Saccharomyces cerevisiae	P32835 (AlphaFold model)
Ankyrin repeat and SOCS box protein 8	C	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

Sequence of entity 1 (A), FASTA

>9OGB_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

>9OGB_2 GTP-binding nuclear protein GSP1/CNR1 (chains B)
GSMSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNF
GEIKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIP
IVLCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEF
V

Sequence of entity 3 (C), FASTA

>9OGB_3 Ankyrin repeat and SOCS box protein 8 (chains C)
GSSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLE
KGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECV
RALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVAL
LVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLA
RYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE

Sequence of entity 4 (E), FASTA

>9OGB_4 Elongin-C (chains E)
MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM
YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC

Sequence of entity 5 (F), FASTA

>9OGB_5 Elongin-B (chains F)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
MG	Magnesium ion	Mg	1
V6A	selinexor, bound form	C17 H13 F6 N7 O	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
9OGE 3.28 Å, Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human…
9OGA 3.37 Å, Cryo-EM structure of human full-length XPO1 conjugated with selinexor

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