Cryo-EM structure of Kap114 bound to H2A-H2B. Determined by electron microscopy at 3.21 Å resolution. Released 26 Jul 2023.
Explore 8F0X in 3D Show helices and sheets RCSB PDB PDBe
8F0X contains 69 α-helices and 8 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 | 3-11 | 9 | |
| α-helix | 15-45 | 31 | |
| α-helix | 51-68 | 18 | |
| α-helix | 84-99 | 16 | |
| α-helix | 105-122 | 18 | |
| α-helix | 130-136 | 7 | |
| α-helix | 137-141 | 5 | |
| α-helix | 144-157 | 14 | |
| α-helix | 160 | 1 | |
| α-helix | 161-165 | 5 | |
| α-helix | 168-181 | 14 | |
| α-helix | 187-205 | 19 | |
| α-helix | 213-234 | 22 | |
| α-helix | 243-262 | 20 | |
| α-helix | 266-268 | 3 | |
| α-helix | 271-291 | 21 | |
| α-helix | 303-320 | 18 | |
| α-helix | 325-327 | 3 | |
| α-helix | 328-341 | 14 | |
| α-helix | 344-345 | 2 | |
| α-helix | 346-354 | 9 | |
| α-helix | 356-363 | 8 | |
| α-helix | 372-380 | 9 | |
| α-helix | 385-402 | 18 | |
| α-helix | 406-420 | 15 | |
| α-helix | 425-426 | 2 | |
| α-helix | 429-447 | 19 | |
| α-helix | 453-469 | 17 | |
| α-helix | 477-493 | 17 | |
| α-helix | 498-514 | 17 | |
| α-helix | 517-541 | 25 | |
| α-helix | 548-561 | 14 | |
| α-helix | 571-587 | 17 | |
| α-helix | 592-604 | 13 | |
| α-helix | 611-631 | 21 | |
| α-helix | 632-635 | 4 | |
| α-helix | 641-655 | 15 | |
| α-helix | 665-681 | 17 | |
| α-helix | 685-701 | 17 | |
| α-helix | 704-707 | 4 | |
| α-helix | 708-710 | 3 | |
| α-helix | 711-722 | 12 | |
| α-helix | 734-744 | 11 | |
| α-helix | 746-749 | 4 | |
| α-helix | 750-752 | 3 | |
| α-helix | 753-766 | 14 | |
| α-helix | 770-786 | 17 | |
| α-helix | 788-797 | 10 | |
| β-strand | 799-800 | 2 | 1 |
| β-strand | 803-804 | 2 | 1 |
| α-helix | 805-816 | 12 | |
| α-helix | 817-819 | 3 | |
| α-helix | 823-839 | 17 | |
| α-helix | 842-845 | 4 | |
| β-strand | 848-854 | 7 | 2 |
| α-helix | 855-856 | 2 | |
| α-helix | 864-866 | 3 | |
| β-strand | 873-878 | 6 | 2 |
| α-helix | 879-894 | 16 | |
| α-helix | 965-977 | 13 | |
| α-helix | 981-983 | 3 | |
| α-helix | 984-990 | 7 | |
| α-helix | 993-999 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-22 | 4 | |
| α-helix | 28-37 | 10 | |
| β-strand | 43-44 | 2 | 3 |
| α-helix | 47-73 | 27 | |
| β-strand | 78-79 | 2 | 4 |
| α-helix | 81-90 | 10 | |
| α-helix | 92-98 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-51 | 11 | |
| β-strand | 56-57 | 2 | 4 |
| α-helix | 59-85 | 27 | |
| α-helix | 86-88 | 3 | |
| β-strand | 91-92 | 2 | 3 |
| α-helix | 94-104 | 11 | |
| α-helix | 108-123 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin subunit beta-5 | A | protein | 1004 | Saccharomyces cerevisiae S288C | P53067 (AlphaFold model) |
| Histone H2A.2 | B | protein | 131 | Saccharomyces cerevisiae S288C | P04912 (AlphaFold model) |
| Histone H2B.2 | C | protein | 130 | Saccharomyces cerevisiae S288C | P02294 (AlphaFold model) |
>8F0X_1 Importin subunit beta-5 (chains A) MDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFALLS LRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQISA VDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEIVFKVL NTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLNFGN VDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVETTES EPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFNTFV SKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYLLQCIL LNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDIKPL TSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRIINQV SSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQSQE CLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLKKKPND GFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKVLER LLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLLSVL CFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLFFLN DKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQSKQPNP EQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITGLMD VKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
>8F0X_2 Histone H2A.2 (chains B) SGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLA AEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKK SAKTAKASQEL
>8F0X_3 Histone H2B.2 (chains C) SSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQK SMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRA VTKYSSSTQA
Mechanism of RanGTP priming H2A-H2B release from Kap114 in an atypical RanGTP•Kap114•H2A-H2B complex. Jiou, J., Shaffer, J.M., Bernades, N.E. et al. Proc Natl Acad Sci U S A (2023) 120:e2301199120-e2301199120. DOI 10.1073/pnas.2301199120 · PubMed
Other PDB entries of the same protein (UniProt P53067 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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