Importin-9 bound to ETS homologous factor (EHF). Determined by electron microscopy at 3.5 Å resolution. Released 27 May 2026.
Explore 10SM in 3D Show helices and sheets RCSB PDB PDBe
10SM contains 70 α-helices and 8 β-strands across 2 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 | 209-218 | 10 | |
| α-helix | 220-222 | 3 | |
| β-strand | 227-231 | 5 | 1 |
| β-strand | 236-239 | 4 | 1 |
| α-helix | 242-253 | 12 | |
| α-helix | 260-268 | 9 | |
| α-helix | 269-273 | 5 | |
| β-strand | 276-278 | 3 | 1 |
| β-strand | 285-288 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-33 | 10 | |
| α-helix | 37-51 | 15 | |
| α-helix | 54-63 | 10 | |
| α-helix | 71-87 | 17 | |
| α-helix | 103-112 | 10 | |
| α-helix | 115-118 | 4 | |
| α-helix | 122-157 | 36 | |
| α-helix | 159-173 | 15 | |
| α-helix | 182-198 | 17 | |
| α-helix | 205-223 | 19 | |
| α-helix | 228-236 | 9 | |
| α-helix | 238-253 | 16 | |
| α-helix | 255 | 1 | |
| α-helix | 262-276 | 15 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-305 | 19 | |
| α-helix | 306-310 | 5 | |
| α-helix | 328-345 | 18 | |
| α-helix | 350-367 | 18 | |
| α-helix | 370-371 | 2 | |
| α-helix | 372-380 | 9 | |
| α-helix | 382-389 | 8 | |
| α-helix | 398-410 | 13 | |
| α-helix | 414-437 | 24 | |
| α-helix | 441-443 | 3 | |
| α-helix | 444-456 | 13 | |
| α-helix | 458-467 | 10 | |
| α-helix | 474-477 | 4 | |
| α-helix | 478-482 | 5 | |
| α-helix | 483-487 | 5 | |
| α-helix | 492-503 | 12 | |
| α-helix | 506-508 | 3 | |
| α-helix | 511-524 | 14 | |
| α-helix | 531-551 | 21 | |
| α-helix | 554-556 | 3 | |
| α-helix | 558-560 | 3 | |
| α-helix | 561-572 | 12 | |
| α-helix | 578-591 | 14 | |
| α-helix | 595-615 | 21 | |
| α-helix | 620-634 | 15 | |
| α-helix | 637-656 | 20 | |
| α-helix | 659-661 | 3 | |
| α-helix | 666-679 | 14 | |
| α-helix | 682 | 1 | |
| α-helix | 685-686 | 2 | |
| α-helix | 687-688 | 2 | |
| α-helix | 689-693 | 5 | |
| α-helix | 694-703 | 10 | |
| α-helix | 707-722 | 16 | |
| α-helix | 725-730 | 6 | |
| β-strand | 732 | 1 | 2 |
| β-strand | 738 | 1 | 2 |
| α-helix | 739-750 | 12 | |
| α-helix | 757-760 | 4 | |
| α-helix | 763-774 | 12 | |
| α-helix | 779-781 | 3 | |
| α-helix | 782-795 | 14 | |
| α-helix | 799-813 | 15 | |
| α-helix | 817-826 | 10 | |
| α-helix | 835-847 | 13 | |
| α-helix | 853-873 | 21 | |
| α-helix | 876-879 | 4 | |
| β-strand | 882-884 | 3 | 3 |
| β-strand | 910-912 | 3 | 3 |
| α-helix | 913-933 | 21 | |
| α-helix | 998-1001 | 4 | |
| α-helix | 1004-1016 | 13 | |
| α-helix | 1021-1027 | 7 | |
| α-helix | 1030-1039 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ETS homologous factor | A | protein | 300 | Homo sapiens | Q9NZC4 (AlphaFold model) |
| Importin-9 | D | protein | 1041 | Homo sapiens | Q96P70 (AlphaFold model) |
>10SM_1 ETS homologous factor (chains A) MILEGGGVMNLNPGNNLLHQPPAWTDSYSTCNVSSGFFGGQWHEIHPQYWTKYQVWEWLQ HLLDTNQLDANCIPFQEFDINGEHLCSMSLQEFTRAAGTAGQLLYSNLQHLKWNGQCSSD LFQSTHNVIVKTEQTEPSIMNTWKDENYLYDTNYGSTVDLLDSKTFCRAQISMTTTSHLP VAESPDMKKEQDPPAKCHTKKHNPRGTHLWEFIRDILLNPDKNPGLIKWEDRSEGVFRFL KSEAVAQLWGKKKNNSSMTYEKLSRAMRYYYKREILERVDGRRLVYKFGKNARGWRENEN
>10SM_2 Importin-9 (chains D) MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHL AELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRES ISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDT QMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPV VQQFTEAFVQALQIPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTE SAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPEL IYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAAA LAAAATRHLQEAEQTKNSGTEHWWKIHEACMLALGSVKAIITDSVKNGRIHFDMHGFLTN VILADLNLSVSPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRA IWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTAS MESKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPAD KIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAY VSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGE NLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVM AEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSK SAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWSQDDSNDMWEDQEEEEEE EEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPC YIMFSGHLNDNERRVLQTIGI
Importin-9 recognizes the winged-helix fold of ETS transcription factors to mediate nuclear import. McConville, M., Lankford, K., Bernardes, N.E. et al. Proc Natl Acad Sci U S A (2026) 123:e2536763123-e2536763123. DOI 10.1073/pnas.2536763123 · PubMed
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