Cryo-EM structure of human importin Beta:Ran-GDP:RanBP1 complex. Determined by electron microscopy at 3.2 Å resolution. Released 10 Dec 2025.
Explore 9YB5 in 3D Show helices and sheets RCSB PDB PDBe
9YB5 contains 40 α-helices and 17 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 | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-63 | 13 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-97 | 13 | |
| α-helix | 108-120 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 163-166 | 4 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-200 | 13 | |
| α-helix | 203-205 | 3 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 249-251 | 3 | |
| α-helix | 260-269 | 10 | |
| α-helix | 273-300 | 28 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-331 | 13 | |
| α-helix | 344-359 | 16 | |
| α-helix | 360-362 | 3 | |
| α-helix | 363-374 | 12 | |
| α-helix | 380-392 | 13 | |
| α-helix | 409-416 | 8 | |
| α-helix | 422-442 | 21 | |
| α-helix | 449-458 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37-50 | 14 | 4 |
| β-strand | 59-72 | 14 | 4 |
| β-strand | 78-83 | 6 | 4 |
| β-strand | 90-95 | 6 | 4 |
| β-strand | 112-119 | 8 | 4 |
| β-strand | 126-133 | 8 | 4 |
| α-helix | 138-159 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-15 | 5 | 1 |
| β-strand | 18 | 1 | 2 |
| β-strand | 20 | 1 | 2 |
| α-helix | 26-31 | 6 | |
| β-strand | 47-54 | 8 | 1 |
| β-strand | 57-65 | 9 | 1 |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 1 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| α-helix | 178-180 | 3 | |
| α-helix | 183-186 | 4 | |
| α-helix | 191-206 | 16 | |
| α-helix | 208-214 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | B | protein | 458 | Homo sapiens | Q14974 (AlphaFold model) |
| GTP-binding nuclear protein Ran | D | protein | 210 | Homo sapiens | P62826 (AlphaFold model) |
| Ran-specific GTPase-activating protein | C | protein | 136 | Homo sapiens | P43487 (AlphaFold model) |
>9YB5_1 Importin subunit beta-1 (chains B) ELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQI KNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEI PVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGM RKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNL VKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAA EQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCED DIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDPS VVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEG
>9YB5_2 GTP-binding nuclear protein Ran (chains D) AAQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWD TAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVD IKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPP EVVMDPALAAQYEHDLEVAQTTALPDEDAA
>9YB5_3 Ran-specific GTPase-activating protein (chains C) PDEQEIATLEEDEEELFCNRAKLFRFASENDLPEWKERGTGDVKLLKHKEKGAIRLLMRR DKTLKICANHYITPMMELKPNAGSDRAWVWNTHADFADECPKPELLAIRFLNAENAQKFK TKFEECRKEIEEREKK
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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