Structure of Importin-4 bound to the H3-H4-ASF1 histone-histone chaperone complex. Determined by electron microscopy at 3.45 Å resolution. Released 21 Sept 2022.
Explore 7UNK in 3D Show helices and sheets RCSB PDB PDBe
7UNK contains 89 α-helices and 18 β-strands across 4 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 | 21-25 | 5 | |
| α-helix | 41-44 | 4 | |
| α-helix | 53-68 | 16 | |
| α-helix | 70-72 | 3 | |
| α-helix | 77-88 | 12 | |
| α-helix | 95-110 | 16 | |
| α-helix | 119-126 | 8 | |
| α-helix | 132-148 | 17 | |
| α-helix | 150-153 | 4 | |
| α-helix | 157-167 | 11 | |
| α-helix | 174-187 | 14 | |
| α-helix | 188-190 | 3 | |
| α-helix | 193-195 | 3 | |
| α-helix | 196-216 | 21 | |
| α-helix | 218-232 | 15 | |
| α-helix | 240-242 | 3 | |
| α-helix | 243-254 | 12 | |
| α-helix | 261-277 | 17 | |
| α-helix | 280-284 | 5 | |
| α-helix | 288-299 | 12 | |
| α-helix | 301-304 | 4 | |
| α-helix | 310-312 | 3 | |
| α-helix | 329-342 | 14 | |
| α-helix | 346-361 | 16 | |
| α-helix | 366-382 | 17 | |
| α-helix | 384-385 | 2 | |
| α-helix | 386-391 | 6 | |
| α-helix | 394-397 | 4 | |
| α-helix | 402-404 | 3 | |
| α-helix | 408-424 | 17 | |
| α-helix | 426-429 | 4 | |
| α-helix | 430-432 | 3 | |
| α-helix | 433-446 | 14 | |
| α-helix | 448 | 1 | |
| α-helix | 452-466 | 15 | |
| α-helix | 470-473 | 4 | |
| α-helix | 477-489 | 13 | |
| α-helix | 495-510 | 16 | |
| α-helix | 519-531 | 13 | |
| α-helix | 535-537 | 3 | |
| α-helix | 538-554 | 17 | |
| α-helix | 557-559 | 3 | |
| α-helix | 560-574 | 15 | |
| α-helix | 580-583 | 4 | |
| α-helix | 587-597 | 11 | |
| α-helix | 599-601 | 3 | |
| α-helix | 602-609 | 8 | |
| α-helix | 613-616 | 4 | |
| β-strand | 622-626 | 5 | 1 |
| α-helix | 629-631 | 3 | |
| β-strand | 643 | 1 | 2 |
| α-helix | 645-647 | 3 | |
| β-strand | 660-665 | 6 | 1 |
| α-helix | 670-686 | 17 | |
| α-helix | 692-704 | 13 | |
| α-helix | 705-707 | 3 | |
| α-helix | 711-734 | 24 | |
| α-helix | 738-757 | 20 | |
| α-helix | 765-781 | 17 | |
| α-helix | 783-785 | 3 | |
| α-helix | 792-804 | 13 | |
| α-helix | 812-815 | 4 | |
| α-helix | 828-846 | 19 | |
| α-helix | 852-865 | 14 | |
| α-helix | 872-889 | 18 | |
| α-helix | 890-893 | 4 | |
| α-helix | 897-907 | 11 | |
| α-helix | 913-929 | 17 | |
| α-helix | 932-937 | 6 | |
| α-helix | 938-951 | 14 | |
| α-helix | 955-970 | 16 | |
| α-helix | 981-987 | 7 | |
| α-helix | 995-997 | 3 | |
| α-helix | 998-1004 | 7 | |
| α-helix | 1020-1032 | 13 | |
| α-helix | 1038-1050 | 13 | |
| α-helix | 1057-1065 | 9 | |
| α-helix | 1068-1076 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 41 | 1 | 1 |
| α-helix | 42-44 | 3 | |
| α-helix | 45-58 | 14 | |
| α-helix | 64-78 | 15 | |
| β-strand | 83-84 | 2 | 3 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 121-130 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 4 |
| β-strand | 16-17 | 2 | 5 |
| α-helix | 21-22 | 2 | |
| β-strand | 25-28 | 4 | 4 |
| β-strand | 38-44 | 7 | 5 |
| β-strand | 55-62 | 8 | 5 |
| α-helix | 77-80 | 4 | |
| α-helix | 86-89 | 4 | |
| β-strand | 92-101 | 10 | 5 |
| β-strand | 104-117 | 14 | 5 |
| α-helix | 120-124 | 5 | |
| α-helix | 132-134 | 3 | |
| β-strand | 135-139 | 5 | 5 |
| β-strand | 145-148 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 3 |
| α-helix | 83-90 | 8 | |
| β-strand | 95-98 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin-4 | A | protein | 1081 | Homo sapiens | Q8TEX9 (AlphaFold model) |
| Histone H3 | C | protein | 136 | Xenopus laevis | Q92133 (AlphaFold model) |
| Histone chaperone | D | protein | 279 | Saccharomyces cerevisiae | P32447 (AlphaFold model) |
| Histone H4 | E | protein | 103 | Xenopus laevis | P62799 (AlphaFold model) |
>7UNK_1 Importin-4 (chains A) MESAGLEQLLRELLLPDTERIRRATEQLQIVLRAPAALPALCDLLASAADPQIRQFAAVL TRRRLNTRWRRLAAEQRESLKSLILTALQRETEHCVSLSLAQLSATIFRKEGLEAWPQLL QLLQHSTHSPHSPEREMGLLLLSVVVTSRPEAFQPHHRELLRLLNETLGEVGSPGLLFYS LRTLTTMAPYLSTEDVPLARMLVPKLIMAMQTLIPIDEAKACEALEALDELLESEVPVIT PYLSEVLTFCLEVARNVALGNAIRIRILCCLTFLVKVKSKALLKNRLLPPLLHTLFPIVA AEPPPGQLDPEDQDSEEEELEIELMGETPKHFAVQVVDMLALHLPPEKLCPQLMPMLEEA LRSESPYQRKAGLLVLAVLSDGAGDHIRQRLLPPLLQIVCKGLEDPSQVVRNAALFALGQ FSENLQPHISSYSREVMPLLLAYLKSVPLGHTHHLAKACYALENFVENLGPKVQPYLPEL MECMLQLLRNPSSPRAKELAVSALGAIATAAQASLLPYFPAIMEHLREFLLTGREDLQPV QIQSLETLGVLARAVGEPMRPLAEECCQLGLGLCDQVDDPDLRRCTYSLFAALSGLMGEG LAPHLEQITTLMLLSLRSTEGIVPQYDGSSSFLLFDDESDGEEEEELMDEDVEEEDDSEI SGYSVENAFFDEKEDTCAAVGEISVNTSVAFLPYMESVFEEVFKLLECPHLNVRKAAHEA LGQFCCALHKACQSCPSEPNTAALQAALARVVPSYMQAVNRERERQVVMAVLEALTGVLR SCGTLTLKPPGRLAELCGVLKAVLQRKTACQDTDEEEEEEDDDQAEYDAMLLEHAGEAIP ALAAAAGGDSFAPFFAGFLPLLVCKTKQGCTVAEKSFAVGTLAETIQGLGAASAQFVSRL LPVLLSTAQEADPEVRSNAIFGMGVLAEHGGHPAQEHFPKLLGLLFPLLARERHDRVRDN ICGALARLLMASPTRKPEPQVLAALLHALPLKEDLEEWVTIGRLFSFLYQSSPDQVIDVA PELLRICSLILADNKIPPDTKAALLLLLTFLAKQHTDSFQAALGSLPVDKAQELQAVLGL S
>7UNK_2 Histone H3 (chains C) MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTE LLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCGIHAKRVTI MPKDIQLARRIRGERA
>7UNK_3 Histone chaperone (chains D) MSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGVDDEEEEDDEEE DDDEDDEDDEDDDQEDGEGEAEEAAEEEEEEEEKTEDNETNLEEEEEDIENSDGDEEEGE EEVGSVDKNEDGNDKKRRKIEGGSTDIESTPKDAARSTN
>7UNK_4 Histone H4 (chains E) MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex. Bernardes, N.E., Fung, H.Y.J., Li, Y. et al. Proc Natl Acad Sci U S A (2022) 119:e2207177119-e2207177119. DOI 10.1073/pnas.2207177119 · PubMed
Other PDB entries of the same protein (UniProt Q8TEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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