Structure of Importin 7 in complex with RanGTP. Determined by electron microscopy at 3.6 Å resolution. Released 23 Sept 2026.
Explore 30JZ in 3D Show helices and sheets RCSB PDB PDBe
30JZ contains 72 α-helices and 11 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 | 3-13 | 11 | |
| α-helix | 19-28 | 10 | |
| α-helix | 35-44 | 10 | |
| α-helix | 50-67 | 18 | |
| α-helix | 79-81 | 3 | |
| α-helix | 85-92 | 8 | |
| α-helix | 95-100 | 6 | |
| α-helix | 104-121 | 18 | |
| α-helix | 128-137 | 10 | |
| α-helix | 143-158 | 16 | |
| α-helix | 164-167 | 4 | |
| α-helix | 168-188 | 21 | |
| α-helix | 194-210 | 17 | |
| α-helix | 222-237 | 16 | |
| α-helix | 239-241 | 3 | |
| α-helix | 242-246 | 5 | |
| α-helix | 252-254 | 3 | |
| α-helix | 256-275 | 20 | |
| α-helix | 286-292 | 7 | |
| α-helix | 293-297 | 5 | |
| α-helix | 298-312 | 15 | |
| α-helix | 319-332 | 14 | |
| α-helix | 336-349 | 14 | |
| α-helix | 350-354 | 5 | |
| α-helix | 355-358 | 4 | |
| α-helix | 362-370 | 9 | |
| α-helix | 372-375 | 4 | |
| α-helix | 376-380 | 5 | |
| α-helix | 389-403 | 15 | |
| α-helix | 408-420 | 13 | |
| α-helix | 426-438 | 13 | |
| α-helix | 440-445 | 6 | |
| α-helix | 447-450 | 4 | |
| α-helix | 453-456 | 4 | |
| α-helix | 457-461 | 5 | |
| α-helix | 462-466 | 5 | |
| α-helix | 470-482 | 13 | |
| α-helix | 491-507 | 17 | |
| α-helix | 511-527 | 17 | |
| α-helix | 529-534 | 6 | |
| α-helix | 539-553 | 15 | |
| α-helix | 556-568 | 13 | |
| α-helix | 570-594 | 25 | |
| α-helix | 601-621 | 21 | |
| α-helix | 626-646 | 21 | |
| α-helix | 649-651 | 3 | |
| α-helix | 652-662 | 11 | |
| α-helix | 669-672 | 4 | |
| α-helix | 674-683 | 10 | |
| α-helix | 690-703 | 14 | |
| α-helix | 705-710 | 6 | |
| α-helix | 713-727 | 15 | |
| α-helix | 732-748 | 17 | |
| α-helix | 757-770 | 14 | |
| α-helix | 776-792 | 17 | |
| α-helix | 794-802 | 9 | |
| β-strand | 806 | 1 | 1 |
| β-strand | 809 | 1 | 1 |
| α-helix | 813-823 | 11 | |
| α-helix | 825-827 | 3 | |
| α-helix | 831-844 | 14 | |
| α-helix | 852-886 | 35 | |
| α-helix | 910-922 | 13 | |
| α-helix | 931-934 | 4 | |
| α-helix | 959-972 | 14 | |
| α-helix | 974-980 | 7 | |
| α-helix | 986-1012 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-17 | 9 | 2 |
| α-helix | 23-31 | 9 | |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 2 |
| β-strand | 57-66 | 10 | 2 |
| α-helix | 78-80 | 3 | |
| β-strand | 85-91 | 7 | 2 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 2 |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 2 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| α-helix | 159-169 | 11 | |
| β-strand | 176 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin 7 L homeolog | A | protein | 1038 | Xenopus laevis | O42480 (AlphaFold model) |
| GTP-binding nuclear protein Ran | B | protein | 175 | Homo sapiens | P62826 (AlphaFold model) |
>30JZ_1 Importin 7 L homeolog (chains A) MDPNILIEALRGTMDPALREAAERQLNESHKSLHFVSTLLQITMSEQLELPVRQAGVIYL KNMITQYWPDREVTPGELPPHTIPEEDRHCIRENIVEAIMHSPELIRVQLTTCIHHIIKH DYPNRWTAVVEKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLIAAMQHFLPM LKDRYIQLLADPSEQSVLIQKQIFKIFYALVQYTLPLELINQQNLAEWIEILKTVVDRDV PAETLQVDEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNDFAEVFLKAFAVGV QQVLLKVLYQYKEKQYIAPRVLQQTLNYFNQGVSHAVTWKNLKPHIQGIIQDVIFPLMCY TDSDEDLWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTSCSKRKEVLQKTMGFCYQILT EPAADPRKKDGALHMIGSLAEILLKKKIYKDQMEFMLQNHVFPLFSSELGYMRARACWVL HYFCEVKFKVDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYIVPFIR PVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEG SDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAH SLTCQQVSPQMWQLLPLVFDIFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYS MCKKILTGVAGEDAECHAAKLLEVVILQCKGRGIDQVIPLFVEAALERLTREVKTSELRT MCLQVAIAALYYSPPLLFNTLENLRFPNNEEPVTNHFIKQWLNDVDCFLGLHDRKICVLG LCALIELEQRPQVLNQMSSQILPAFLLLFNGLKRAYACHAEQENDSDDDGDGEDDEDAAE LGSDEDDIDEEGQEYLEILAKQAGEDGDDEDWEDDDAEETALEGYTTLLDDEDTPIDEYQ IFKAIFQKLQGRDPVWYQALTQGLNEDQGKQLQDIATLADQRRAAHESKMIEKHGGYKFN APVVPSTFNFGNPAPGMN
>30JZ_2 GTP-binding nuclear protein Ran (chains B) EPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWD TAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVD IKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
Chaperoning by dynamic encasement: Structural basis of linker histone H1 nuclear import. Fu, Z., Chafra, F., Freytag, B. et al. Structure (2026). DOI 10.1016/j.str.2026.09.001
Other PDB entries of the same protein (UniProt O42480 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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