Cryo-EM structure of human importin beta:importin alpha (IBB) complex. Determined by electron microscopy at 3.3 Å resolution. Released 10 Dec 2025.
Explore 9N86 in 3D Show helices and sheets RCSB PDB PDBe
9N86 contains 55 α-helices and 0 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 | 3-11 | 9 | |
| α-helix | 16-30 | 15 | |
| α-helix | 33-44 | 12 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 109-120 | 12 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 164-166 | 3 | |
| α-helix | 170-179 | 10 | |
| α-helix | 189-200 | 12 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-226 | 15 | |
| α-helix | 231-247 | 17 | |
| α-helix | 250-253 | 4 | |
| α-helix | 256-269 | 14 | |
| α-helix | 273-302 | 30 | |
| α-helix | 306-307 | 2 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-329 | 11 | |
| α-helix | 344-358 | 15 | |
| α-helix | 364-373 | 10 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-416 | 18 | |
| α-helix | 422-438 | 17 | |
| α-helix | 440-443 | 4 | |
| α-helix | 446-459 | 14 | |
| α-helix | 464-484 | 21 | |
| α-helix | 498-500 | 3 | |
| α-helix | 503-514 | 12 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-537 | 14 | |
| α-helix | 544-566 | 23 | |
| α-helix | 571-594 | 24 | |
| α-helix | 597-616 | 20 | |
| α-helix | 622-639 | 18 | |
| α-helix | 640-646 | 7 | |
| α-helix | 647-658 | 12 | |
| α-helix | 664-680 | 17 | |
| α-helix | 686-701 | 16 | |
| α-helix | 709-724 | 16 | |
| α-helix | 726-730 | 5 | |
| α-helix | 732-743 | 12 | |
| α-helix | 752-777 | 26 | |
| α-helix | 783-784 | 2 | |
| α-helix | 787-793 | 7 | |
| α-helix | 794-806 | 13 | |
| α-helix | 812-828 | 17 | |
| α-helix | 831-839 | 9 | |
| α-helix | 841-843 | 3 | |
| α-helix | 844-852 | 9 | |
| α-helix | 856-873 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| α-helix | 24-50 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| Importin subunit alpha-1 | B | protein | 53 | Homo sapiens | P52292 (AlphaFold model) |
>9N86_1 Importin subunit beta-1 (chains A) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>9N86_2 Importin subunit alpha-1 (chains B) MSTNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNV
Ran modulates allosteric crosstalk between importin beta surfaces. Ko, Y.H., Li, F., Suinn, S.S. et al. Nat Commun (2025) 16:11425-11425. DOI 10.1038/s41467-025-66255-0 · PubMed
Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9N86 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.