Cryo-EM structure of human importin beta-Ran-GTP heterodimer. Determined by electron microscopy at 3.3 Å resolution. Released 8 Oct 2025.
Explore 9BAW in 3D Show helices and sheets RCSB PDB PDBe
9BAW contains 59 α-helices and 9 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 | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-44 | 12 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 109-123 | 15 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-201 | 14 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 249-251 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-268 | 8 | |
| α-helix | 273-302 | 30 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-329 | 11 | |
| α-helix | 344-359 | 16 | |
| α-helix | 360-362 | 3 | |
| α-helix | 364-374 | 11 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-417 | 19 | |
| α-helix | 422-438 | 17 | |
| α-helix | 440-443 | 4 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-483 | 20 | |
| α-helix | 498-501 | 4 | |
| α-helix | 503-514 | 12 | |
| α-helix | 521-523 | 3 | |
| α-helix | 524-537 | 14 | |
| α-helix | 541-543 | 3 | |
| α-helix | 544-562 | 19 | |
| α-helix | 571-592 | 22 | |
| α-helix | 597-617 | 21 | |
| α-helix | 627-639 | 13 | |
| α-helix | 641-645 | 5 | |
| α-helix | 647-660 | 14 | |
| α-helix | 664-681 | 18 | |
| α-helix | 682-685 | 4 | |
| α-helix | 686-698 | 13 | |
| α-helix | 709-724 | 16 | |
| α-helix | 725-730 | 6 | |
| α-helix | 732-744 | 13 | |
| α-helix | 753-776 | 24 | |
| α-helix | 785-789 | 5 | |
| α-helix | 793-806 | 14 | |
| α-helix | 812-829 | 18 | |
| α-helix | 831-838 | 8 | |
| α-helix | 841-852 | 12 | |
| α-helix | 856-875 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-16 | 6 | 1 |
| α-helix | 23-31 | 9 | |
| β-strand | 45-54 | 10 | 1 |
| β-strand | 57-66 | 10 | 1 |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 1 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 1 |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 1 |
| β-strand | 150 | 1 | 2 |
| β-strand | 155 | 1 | 2 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-1 | A | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| GTP-binding nuclear protein Ran | B | protein | 170 | Homo sapiens | P62826 (AlphaFold model) |
>9BAW_1 Importin subunit beta-1 (chains A) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLHTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLARWATKELRKLKNQA
>9BAW_2 GTP-binding nuclear protein Ran (chains B) VQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAG QEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKD RKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFAA
Cryo-EM structure of human importin beta-Ran-GTP heterodimer. Ko, Y., Cingolani, G. To be published.
Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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