Cryo-EM structure of human exportin-1 conjugated with KPT-UTSW1 and bound to human ASB8-ELOB/C. Determined by electron microscopy at 4.21 Å resolution. Released 26 Nov 2025.
Explore 9OGF in 3D Show helices and sheets RCSB PDB PDBe
9OGF contains 67 α-helices and 18 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 264-273 | 10 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-292 | 13 | |
| α-helix | 304-309 | 6 | |
| α-helix | 317-323 | 7 | |
| α-helix | 327-338 | 12 | |
| α-helix | 344-347 | 4 | |
| α-helix | 351-358 | 8 | |
| α-helix | 364-383 | 20 | |
| α-helix | 410-423 | 14 | |
| α-helix | 453-467 | 15 | |
| α-helix | 469-484 | 16 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 534-549 | 16 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-573 | 15 | |
| α-helix | 580-594 | 15 | |
| α-helix | 596-599 | 4 | |
| α-helix | 610-621 | 12 | |
| α-helix | 622-624 | 3 | |
| α-helix | 627-642 | 16 | |
| α-helix | 647-674 | 28 | |
| α-helix | 676-678 | 3 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-735 | 29 | |
| α-helix | 736-739 | 4 | |
| α-helix | 743-764 | 22 | |
| α-helix | 769-771 | 3 | |
| α-helix | 772-776 | 5 | |
| α-helix | 777-790 | 14 | |
| α-helix | 799-811 | 13 | |
| α-helix | 814-818 | 5 | |
| α-helix | 819-822 | 4 | |
| α-helix | 823-827 | 5 | |
| α-helix | 828-834 | 7 | |
| α-helix | 842-858 | 17 | |
| α-helix | 860-865 | 6 | |
| α-helix | 868-882 | 15 | |
| α-helix | 896-904 | 9 | |
| α-helix | 914 | 1 | |
| α-helix | 915-919 | 5 | |
| α-helix | 920-926 | 7 | |
| α-helix | 946-953 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 89-96 | 8 | |
| α-helix | 98-106 | 9 | |
| α-helix | 121-128 | 8 | |
| α-helix | 131-139 | 9 | |
| α-helix | 154-161 | 8 | |
| α-helix | 165-172 | 8 | |
| α-helix | 187-196 | 10 | |
| α-helix | 204-215 | 12 | |
| α-helix | 241-245 | 5 | |
| α-helix | 250-262 | 13 | |
| α-helix | 267-273 | 7 | |
| α-helix | 278-284 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 1 |
| α-helix | 67-82 | 16 | |
| α-helix | 97-110 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 2 |
| β-strand | 5-9 | 5 | 1 |
| β-strand | 10 | 1 | 3 |
| β-strand | 12-13 | 2 | 1 |
| β-strand | 18 | 1 | 2 |
| β-strand | 23 | 1 | 4 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 49-50 | 2 | 1 |
| β-strand | 56 | 1 | 4 |
| β-strand | 68 | 1 | 5 |
| β-strand | 71 | 1 | 5 |
| β-strand | 73-79 | 7 | 1 |
| β-strand | 80 | 1 | 6 |
| β-strand | 85 | 1 | 6 |
| α-helix | 86-87 | 2 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-96 | 5 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-103 | 3 |
| 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) |
>9OGF_1 Exportin-1 (chains A) GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV FDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQML PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVS EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRL LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTE KLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILF TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI STSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF LVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
>9OGF_2 Ankyrin repeat and SOCS box protein 8 (chains B) GSSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLE KGAEVNALDGYNRTALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECV RALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLIGQTPISRLVAL LVRGLGTEKEDSCFELLHRAVGHFELRKNGTMPREVARDPQLCEKLTVLCSAPGTLKTLA RYAVRRSLGLQYLPDAVKGLPLPASLKEYLLLLE
>9OGF_3 Elongin-C (chains E) MMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCM YFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
>9OGF_4 Elongin-B (chains F) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CBB | propan-2-yl 3-(3-phenyl-1H-1,2,4-triazol-1-yl)propanoate | C14 H17 N3 O2 | 1 |
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:
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