Cryo-EM structure of human importin beta: xIBB complex. Determined by electron microscopy at 3.4 Å resolution. Released 10 Dec 2025.
Explore 9N87 in 3D Show helices and sheets RCSB PDB PDBe
9N87 contains 62 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 | 16-21 | 6 | |
| α-helix | 23-24 | 2 | |
| α-helix | 25-29 | 5 | |
| α-helix | 37-40 | 4 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 92-98 | 7 | |
| α-helix | 109-120 | 12 | |
| α-helix | 129-134 | 6 | |
| α-helix | 135-137 | 3 | |
| α-helix | 144-160 | 17 | |
| α-helix | 165-169 | 5 | |
| α-helix | 170-177 | 8 | |
| α-helix | 189-201 | 13 | |
| α-helix | 206-209 | 4 | |
| α-helix | 212-224 | 13 | |
| α-helix | 231-241 | 11 | |
| α-helix | 245-248 | 4 | |
| α-helix | 249-254 | 6 | |
| α-helix | 256-261 | 6 | |
| α-helix | 262-268 | 7 | |
| α-helix | 273-303 | 31 | |
| α-helix | 306-307 | 2 | |
| α-helix | 314-317 | 4 | |
| α-helix | 323-330 | 8 | |
| α-helix | 344-359 | 16 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-374 | 12 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-416 | 18 | |
| α-helix | 423-438 | 16 | |
| α-helix | 440-443 | 4 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-470 | 7 | |
| α-helix | 478-483 | 6 | |
| α-helix | 500-514 | 15 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-537 | 14 | |
| α-helix | 544-560 | 17 | |
| α-helix | 571-592 | 22 | |
| α-helix | 597-615 | 19 | |
| α-helix | 622-639 | 18 | |
| α-helix | 641-643 | 3 | |
| α-helix | 644-658 | 15 | |
| α-helix | 664-672 | 9 | |
| α-helix | 673-677 | 5 | |
| α-helix | 678-681 | 4 | |
| α-helix | 689-701 | 13 | |
| α-helix | 709-724 | 16 | |
| α-helix | 732-743 | 12 | |
| α-helix | 752-777 | 26 | |
| α-helix | 783-784 | 2 | |
| α-helix | 785-793 | 9 | |
| α-helix | 794-806 | 13 | |
| α-helix | 814-822 | 9 | |
| α-helix | 825-828 | 4 | |
| α-helix | 833-836 | 4 | |
| α-helix | 842-850 | 9 | |
| α-helix | 856-873 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-41 | 21 | |
| α-helix | 42-44 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| XRIP1a | B | protein | 45 | Xenopus laevis | A0A2I3HSY1 (AlphaFold model) |
>9N87_1 Importin subunit beta-1 (chains A) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>9N87_2 XRIP1a (chains B) MAESLRSPRRSLYKLVGSPPWKEAFRQRCLERMRNSRDRLLNRYR
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:
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