Cryo-EM structure of the Importin7:Importin beta:Histone H1.0 complex. Determined by electron microscopy at 6.2 Å resolution. Released 27 Feb 2019.
Explore 6N88 in 3D Show helices and sheets RCSB PDB PDBe
6N88 contains 95 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 | 293-309 | 17 | |
| α-helix | 320-322 | 3 | |
| α-helix | 323-340 | 18 | |
| α-helix | 344-366 | 23 | |
| α-helix | 382-403 | 22 | |
| α-helix | 410-420 | 11 | |
| α-helix | 429-433 | 5 | |
| α-helix | 434-439 | 6 | |
| α-helix | 440-444 | 5 | |
| α-helix | 445-449 | 5 | |
| α-helix | 458-464 | 7 | |
| α-helix | 472-482 | 11 | |
| α-helix | 493-506 | 14 | |
| α-helix | 511-526 | 16 | |
| α-helix | 535-552 | 18 | |
| α-helix | 556-570 | 15 | |
| α-helix | 574-600 | 27 | |
| α-helix | 605-620 | 16 | |
| α-helix | 625-627 | 3 | |
| α-helix | 629-646 | 18 | |
| α-helix | 654-661 | 8 | |
| α-helix | 669-688 | 20 | |
| α-helix | 690-707 | 18 | |
| α-helix | 715-726 | 12 | |
| α-helix | 729-731 | 3 | |
| α-helix | 736-750 | 15 | |
| α-helix | 751-753 | 3 | |
| α-helix | 757-773 | 17 | |
| α-helix | 779-791 | 13 | |
| α-helix | 794-795 | 2 | |
| α-helix | 796-801 | 6 | |
| α-helix | 802-803 | 2 | |
| α-helix | 811-826 | 16 | |
| α-helix | 829-831 | 3 | |
| α-helix | 835-847 | 13 | |
| α-helix | 851-869 | 19 | |
| α-helix | 959-972 | 14 | |
| α-helix | 975-979 | 5 | |
| α-helix | 982-996 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-9 | 5 | |
| α-helix | 17-21 | 5 | |
| α-helix | 22 | 1 | |
| α-helix | 23-29 | 7 | |
| α-helix | 30-35 | 6 | |
| α-helix | 37-45 | 9 | |
| α-helix | 52-56 | 5 | |
| α-helix | 57-62 | 6 | |
| α-helix | 70-73 | 4 | |
| α-helix | 76-82 | 7 | |
| α-helix | 88-101 | 14 | |
| α-helix | 108-120 | 13 | |
| α-helix | 129-137 | 9 | |
| α-helix | 144-149 | 6 | |
| α-helix | 152-159 | 8 | |
| α-helix | 168-182 | 15 | |
| α-helix | 188-202 | 15 | |
| α-helix | 209-210 | 2 | |
| α-helix | 213-227 | 15 | |
| α-helix | 232-247 | 16 | |
| α-helix | 258-269 | 12 | |
| α-helix | 278-300 | 23 | |
| α-helix | 319-322 | 4 | |
| α-helix | 325-329 | 5 | |
| α-helix | 344-357 | 14 | |
| α-helix | 363-376 | 14 | |
| α-helix | 380-393 | 14 | |
| α-helix | 399-414 | 16 | |
| α-helix | 422-438 | 17 | |
| α-helix | 445-457 | 13 | |
| α-helix | 468-485 | 18 | |
| α-helix | 496-514 | 19 | |
| α-helix | 517-518 | 2 | |
| α-helix | 525-537 | 13 | |
| α-helix | 544-566 | 23 | |
| α-helix | 572-592 | 21 | |
| α-helix | 597-621 | 25 | |
| α-helix | 625-636 | 12 | |
| α-helix | 643-659 | 17 | |
| α-helix | 667-680 | 14 | |
| α-helix | 688-705 | 18 | |
| α-helix | 711-721 | 11 | |
| α-helix | 729-744 | 16 | |
| α-helix | 746-747 | 2 | |
| β-strand | 750 | 1 | 1 |
| β-strand | 753 | 1 | 1 |
| α-helix | 758-775 | 18 | |
| α-helix | 787-791 | 5 | |
| α-helix | 792-796 | 5 | |
| α-helix | 797-806 | 10 | |
| α-helix | 812-829 | 18 | |
| α-helix | 834-838 | 5 | |
| α-helix | 840-851 | 12 | |
| α-helix | 859-870 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-38 | 11 | |
| α-helix | 47-57 | 11 | |
| α-helix | 64-68 | 5 | |
| α-helix | 69-77 | 9 | |
| β-strand | 81-87 | 7 | 2 |
| β-strand | 90-95 | 6 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MGC52556 protein | 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 | 194 | Homo sapiens | P07305 (AlphaFold model) |
>6N88_1 MGC52556 protein (chains A) MDPNILIEALRGTMDPALREAAERQLNESHKSLHFVSTLLQITMSEQLELPVRQAGVIYL KNMITQYWPDREVTPGELPPHTIPEEDRHCIRENIVEAIMHSPELIRVQLTTCIHHIIKH DYPNRWTAVVEKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLIAAMQHFLPM LKDRYIQLLADPSEQSVLIQKQIFKIFYALVQYTLPLELINQQNLAEWIEILKTVVDRDV PAETLQVDEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNDFAEVFLKAFAVGV QQVLLKVLYQYKEKQYIAPRVLQQTLNYFNQGVSHAVTWKNLKPHIQGIIQDVIFPLMCY TDSDEDLWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTSCSKRKEVLQKTMGFCYQILT EPAADPRKKDGALHMIGSLAEILLKKKIYKDQMEFMLQNHVFPLFSSELGYMRARACWVL HYFCEVKFKVDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYIVPFIR PVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEG SDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAH SLTCQQVSPQMWQLLPLVFDIFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYS MCKKILTGVAGEDAECHAAKLLEVVILQCKGRGIDQVIPLFVEAALERLTREVKTSELRT MCLQVAIAALYYSPPLLFNTLENLRFPNNEEPVTNHFIKQWLNDVDCFLGLHDRKICVLG LCALIELEQRPQVLNQMSSQILPAFLLLFNGLKRAYACHAEQENDSDDDGDGEDDEDAAE LGSDEDDIDEEGQEYLEILAKQAGEDGDDEDWEDDDAEETALEGYTTLLDDEDTPIDEYQ IFKAIFQKLQGRDPVWYQALTQGLNEDQGKQLQDIATLADQRRAAHESKMIEKHGGYKFN APVVPSTFNFGNPAPGMN
>6N88_2 Importin subunit beta-1 (chains B) MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
>6N88_3 Histone H1.0 (chains C) MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKV GENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATP KKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVK PKAKSSAKRAGKKK
Fuzzy Interactions Form and Shape the Histone Transport Complex. Ivic, N., Potocnjak, M., Solis-Mezarino, V. et al. Mol Cell (2019) 73:1191. DOI 10.1016/j.molcel.2019.01.032 · PubMed
Other PDB entries of the same protein (UniProt O42480 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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