Binary complex of human Importin-9 with one homodimer of Akirin-2. Determined by electron microscopy at 3.7 Å resolution. Released 28 Jan 2026.
Explore 9QOP in 3D Show helices and sheets RCSB PDB PDBe
9QOP contains 72 α-helices and 6 β-strands across 3 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 | 17-33 | 17 | |
| α-helix | 37-51 | 15 | |
| α-helix | 56-65 | 10 | |
| α-helix | 71-88 | 18 | |
| α-helix | 103-112 | 10 | |
| α-helix | 113-116 | 4 | |
| α-helix | 123-137 | 15 | |
| α-helix | 146-157 | 12 | |
| α-helix | 160-173 | 14 | |
| α-helix | 182-189 | 8 | |
| α-helix | 205-225 | 21 | |
| α-helix | 234-237 | 4 | |
| α-helix | 241-251 | 11 | |
| α-helix | 254-256 | 3 | |
| α-helix | 262-275 | 14 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-305 | 19 | |
| α-helix | 306-310 | 5 | |
| α-helix | 329-342 | 14 | |
| α-helix | 350-364 | 15 | |
| α-helix | 365-368 | 4 | |
| α-helix | 369-371 | 3 | |
| α-helix | 372-378 | 7 | |
| α-helix | 382-387 | 6 | |
| α-helix | 398-412 | 15 | |
| α-helix | 418-428 | 11 | |
| α-helix | 432-437 | 6 | |
| α-helix | 444-456 | 13 | |
| α-helix | 458-465 | 8 | |
| α-helix | 474-477 | 4 | |
| α-helix | 478-482 | 5 | |
| α-helix | 483-486 | 4 | |
| α-helix | 492-504 | 13 | |
| α-helix | 506-508 | 3 | |
| α-helix | 511-522 | 12 | |
| α-helix | 530 | 1 | |
| α-helix | 535-551 | 17 | |
| α-helix | 561-573 | 13 | |
| α-helix | 577-591 | 15 | |
| α-helix | 595-600 | 6 | |
| α-helix | 602-615 | 14 | |
| α-helix | 620-635 | 16 | |
| α-helix | 643-656 | 14 | |
| α-helix | 666-680 | 15 | |
| α-helix | 687 | 1 | |
| α-helix | 688-693 | 6 | |
| α-helix | 694-703 | 10 | |
| α-helix | 707-723 | 17 | |
| α-helix | 725-730 | 6 | |
| β-strand | 732 | 1 | 2 |
| β-strand | 738 | 1 | 2 |
| α-helix | 739-751 | 13 | |
| α-helix | 757-762 | 6 | |
| α-helix | 763-770 | 8 | |
| α-helix | 776-780 | 5 | |
| α-helix | 782-792 | 11 | |
| α-helix | 793-795 | 3 | |
| α-helix | 799-813 | 15 | |
| α-helix | 817-826 | 10 | |
| α-helix | 828-829 | 2 | |
| α-helix | 835-840 | 6 | |
| α-helix | 853-867 | 15 | |
| α-helix | 898-901 | 4 | |
| α-helix | 904-907 | 4 | |
| α-helix | 913-935 | 23 | |
| α-helix | 992-995 | 4 | |
| α-helix | 998-1000 | 3 | |
| α-helix | 1004-1016 | 13 | |
| α-helix | 1022-1025 | 4 | |
| α-helix | 1030-1032 | 3 | |
| α-helix | 1033-1038 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 142 | 1 | 1 |
| α-helix | 144-191 | 48 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 70 | 1 | 3 |
| β-strand | 73 | 1 | 3 |
| α-helix | 77-90 | 14 | |
| β-strand | 142 | 1 | 1 |
| α-helix | 144-191 | 48 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Akirin-2 | B, C | protein | 203 | Homo sapiens | Q53H80 (AlphaFold model) |
| Importin-9 | A | protein | 1041 | Homo sapiens | Q96P70 (AlphaFold model) |
>9QOP_1 Akirin-2 (chains B, C) MACGATLKRTLDFDPLLSPASPKRRRCAPLSAPTSAAASPLSAAAATAASFSAAAASPQK YLRMEPSPFGDVSSRLTTEQILYNIKQEYKRMQKRRHLETSFQQTDPCCTSDAQPHAFLL SGPASPGTSSAASSPLKKEQPLFTLRQVGMICERLLKEREEKVREEYEEILNTKLAEQYD AFVKFTHDQIMRRYGEQPASYVS
>9QOP_2 Importin-9 (chains A) MAAAAAAGAASGLPGPVAQGLKEALVDTLTGILSPVQEVRAAAEEQIKVLEVTEEFGVHL AELTVDPQGALAIRQLASVILKQYVETHWCAQSEKFRPPETTERAKIVIRELLPNGLRES ISKVRSSVAYAVSAIAHWDWPEAWPQLFNLLMEMLVSGDLNAVHGAMRVLTEFTREVTDT QMPLVAPVILPEMYKIFTMAEVYGIRTRSRAVEIFTTCAHMICNMEELEKGAAKVLIFPV VQQFTEAFVQALQIPDGPTSDSGFKMEVLKAVTALVKNFPKHMVSSMQQILPIVWNTLTE SAAFYVRTEVNYTEEVEDPVDSDGEVLGFENLVFSIFEFVHALLENSKFKSTVKKALPEL IYYIILYMQITEEQIKVWTANPQQFVEDEDDDTFSYTVRIAAQDLLLAVATDFQNESAAA LAAAATRHLQEAEQTKNSGTEHWWKIHEACMLALGSVKAIITDSVKNGRIHFDMHGFLTN VILADLNLSVSPFLLGRALWAASRFTVAMSPELIQQFLQATVSGLHETQPPSVRISAVRA IWGYCDQLKVSESTHVLQPFLPSILDGLIHLAAQFSSEVLNLVMETLCIVCTVDPEFTAS MESKICPFTIAIFLKYSNDPVVASLAQDIFKELSQIEACQGPMQMRLIPTLVSIMQAPAD KIPAGLCATAIDILTTVVRNTKPPLSQLLICQAFPAVAQCTLHTDDNATMQNGGECLRAY VSVTLEQVAQWHDEQGHNGLWYVMQVVSQLLDPRTSEFTAAFVGRLVSTLISKAGRELGE NLDQILRAILSKMQQAETLSVMQSLIMVFAHLVHTQLEPLLEFLCSLPGPTGKPALEFVM AEWTSRQHLFYGQYEGKVSSVALCKLLQHGINADDKRLQDIRVKGEEIYSMDEGIRTRSK SAKNPERWTNIPLLVKILKLIINELSNVMEANAARQATPAEWSQDDSNDMWEDQEEEEEE EEDGLAGQLLSDILATSKYEEDYYEDDEEDDPDALKDPLYQIDLQAYLTDFLCQFAQQPC YIMFSGHLNDNERRVLQTIGI
A multivalent adaptor mechanism drives the nuclear import of proteasomes. Brunner, H.L., Kalis, R.W., Grundmann, L. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69162-0 · PubMed
Other PDB entries of the same protein (UniProt Q53H80 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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