Structure of importin beta bound to the ibb domain of importin alpha. Determined by X-ray diffraction at 2.5 Å resolution. Released 24 May 1999.
Explore 1QGK in 3D Show helices and sheets RCSB PDB PDBe
1QGK contains 64 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 | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-44 | 12 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-96 | 12 | |
| α-helix | 108-120 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 163-165 | 3 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-201 | 14 | |
| α-helix | 202-204 | 3 | |
| α-helix | 206-209 | 4 | |
| α-helix | 212-225 | 14 | |
| α-helix | 231-247 | 17 | |
| α-helix | 249-251 | 3 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-268 | 8 | |
| α-helix | 273-302 | 30 | |
| α-helix | 314-329 | 16 | |
| α-helix | 330-332 | 3 | |
| α-helix | 344-359 | 16 | |
| α-helix | 360-363 | 4 | |
| α-helix | 364-374 | 11 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-407 | 9 | |
| α-helix | 410-416 | 7 | |
| α-helix | 422-438 | 17 | |
| α-helix | 440-442 | 3 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-485 | 22 | |
| α-helix | 486-488 | 3 | |
| α-helix | 500-502 | 3 | |
| 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 | 600-616 | 17 | |
| α-helix | 622-639 | 18 | |
| α-helix | 640-643 | 4 | |
| α-helix | 644-660 | 17 | |
| α-helix | 664-681 | 18 | |
| α-helix | 682-685 | 4 | |
| α-helix | 686-700 | 15 | |
| α-helix | 707-709 | 3 | |
| α-helix | 710-724 | 15 | |
| α-helix | 725-728 | 4 | |
| α-helix | 732-743 | 12 | |
| α-helix | 752-755 | 4 | |
| α-helix | 758-776 | 19 | |
| α-helix | 786-789 | 4 | |
| α-helix | 791-793 | 3 | |
| α-helix | 794-806 | 13 | |
| α-helix | 812-829 | 18 | |
| α-helix | 831-837 | 7 | |
| α-helix | 842-852 | 11 | |
| α-helix | 856-873 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-16 | 3 | |
| α-helix | 24-51 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (importin beta subunit) | A | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| Protein (importin alpha-2 subunit) | B | protein | 44 | P52292 (AlphaFold model) |
>1QGK_1 PROTEIN (IMPORTIN BETA SUBUNIT) (chains A) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLHTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLARWATKELRKLKNQA
>1QGK_2 PROTEIN (IMPORTIN ALPHA-2 SUBUNIT) (chains B) AARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVS
Structure of importin-beta bound to the IBB domain of importin-alpha. Cingolani, G., Petosa, C., Weis, K. et al. Nature (1999) 399:221-229. DOI 10.1038/20367 · 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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