Structure of histone H1 in an import-chaperone complex with importin beta and importin 7 (full-length model). Determined by electron microscopy at 3.6 Å resolution. Released 23 Sept 2026.
Explore 30FM in 3D Show helices and sheets RCSB PDB PDBe
30FM contains 125 α-helices and 4 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 | 3-13 | 11 | |
| α-helix | 16-18 | 3 | |
| α-helix | 19-30 | 12 | |
| α-helix | 35-44 | 10 | |
| α-helix | 50-67 | 18 | |
| α-helix | 78-81 | 4 | |
| α-helix | 85-101 | 17 | |
| α-helix | 104-121 | 18 | |
| α-helix | 128-137 | 10 | |
| α-helix | 142-158 | 17 | |
| α-helix | 164-190 | 27 | |
| α-helix | 194-211 | 18 | |
| α-helix | 222-237 | 16 | |
| α-helix | 239-240 | 2 | |
| α-helix | 249-251 | 3 | |
| α-helix | 256-270 | 15 | |
| α-helix | 271-275 | 5 | |
| α-helix | 283-295 | 13 | |
| α-helix | 297-312 | 16 | |
| 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 | 372-378 | 7 | |
| α-helix | 382-387 | 6 | |
| α-helix | 389-403 | 15 | |
| α-helix | 408-420 | 13 | |
| α-helix | 426-438 | 13 | |
| α-helix | 440-445 | 6 | |
| α-helix | 450-456 | 7 | |
| α-helix | 457-461 | 5 | |
| α-helix | 462-466 | 5 | |
| α-helix | 470-482 | 13 | |
| α-helix | 491-506 | 16 | |
| α-helix | 511-527 | 17 | |
| α-helix | 531-535 | 5 | |
| α-helix | 536-538 | 3 | |
| α-helix | 539-553 | 15 | |
| α-helix | 556-568 | 13 | |
| α-helix | 570-573 | 4 | |
| α-helix | 574-576 | 3 | |
| α-helix | 577-594 | 18 | |
| α-helix | 595-597 | 3 | |
| α-helix | 601-621 | 21 | |
| α-helix | 626-645 | 20 | |
| α-helix | 649-651 | 3 | |
| α-helix | 652-663 | 12 | |
| α-helix | 671-673 | 3 | |
| α-helix | 674-684 | 11 | |
| α-helix | 687-689 | 3 | |
| α-helix | 690-702 | 13 | |
| α-helix | 705-710 | 6 | |
| α-helix | 712-727 | 16 | |
| α-helix | 732-748 | 17 | |
| α-helix | 758-770 | 13 | |
| α-helix | 776-792 | 17 | |
| α-helix | 794-803 | 10 | |
| α-helix | 813-823 | 11 | |
| α-helix | 825-827 | 3 | |
| α-helix | 831-845 | 15 | |
| α-helix | 852-856 | 5 | |
| α-helix | 858-860 | 3 | |
| α-helix | 861-884 | 24 | |
| α-helix | 910-923 | 14 | |
| α-helix | 958-972 | 15 | |
| α-helix | 974-981 | 8 | |
| α-helix | 986-1013 | 28 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-9 | 7 | |
| α-helix | 15-31 | 17 | |
| α-helix | 33-45 | 13 | |
| α-helix | 51-65 | 15 | |
| α-helix | 70-81 | 12 | |
| α-helix | 85-98 | 14 | |
| α-helix | 108-120 | 13 | |
| α-helix | 121-123 | 3 | |
| α-helix | 129-138 | 10 | |
| α-helix | 144-160 | 17 | |
| α-helix | 170-181 | 12 | |
| α-helix | 188-200 | 13 | |
| α-helix | 206-210 | 5 | |
| α-helix | 212-226 | 15 | |
| α-helix | 231-247 | 17 | |
| α-helix | 253-255 | 3 | |
| α-helix | 256-260 | 5 | |
| α-helix | 261-269 | 9 | |
| α-helix | 273-302 | 30 | |
| α-helix | 314-329 | 16 | |
| α-helix | 344-359 | 16 | |
| α-helix | 360-363 | 4 | |
| α-helix | 364-374 | 11 | |
| α-helix | 380-392 | 13 | |
| α-helix | 399-416 | 18 | |
| α-helix | 422-438 | 17 | |
| α-helix | 440-443 | 4 | |
| α-helix | 449-459 | 11 | |
| α-helix | 464-484 | 21 | |
| 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 | 544-563 | 20 | |
| α-helix | 571-594 | 24 | |
| α-helix | 597-617 | 21 | |
| α-helix | 622-639 | 18 | |
| α-helix | 644-659 | 16 | |
| α-helix | 664-681 | 18 | |
| α-helix | 682-684 | 3 | |
| α-helix | 686-701 | 16 | |
| α-helix | 709-724 | 16 | |
| α-helix | 725-730 | 6 | |
| α-helix | 732-744 | 13 | |
| α-helix | 752-777 | 26 | |
| α-helix | 785-793 | 9 | |
| α-helix | 794-806 | 13 | |
| α-helix | 812-828 | 17 | |
| α-helix | 831-838 | 8 | |
| α-helix | 841-852 | 12 | |
| α-helix | 856-874 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-38 | 11 | |
| β-strand | 45 | 1 | 1 |
| α-helix | 47-57 | 11 | |
| α-helix | 64-78 | 15 | |
| β-strand | 81-82 | 2 | 2 |
| β-strand | 93 | 1 | 1 |
| β-strand | 94-95 | 2 | 2 |
| α-helix | 183-185 | 3 | |
| α-helix | 188-189 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin 7 L homeolog | A | protein | 1038 | Xenopus laevis | O42480 (AlphaFold model) |
| Importin subunit beta-1 | B | protein | 876 | Homo sapiens | Q14974 (AlphaFold model) |
| Histone H1.0 | C | protein | 195 | Homo sapiens | P07305 (AlphaFold model) |
>30FM_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
>30FM_2 Importin subunit beta-1 (chains B) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>30FM_3 Histone H1.0 (chains C) GMTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYK VGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVAT PKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPV KPKAKSSAKRAGKKK
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:
MolViewer shows 30FM directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.