Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114. Determined by electron microscopy at 3.54 Å resolution. Released 27 Nov 2024.
Explore 9B3F in 3D Show helices and sheets RCSB PDB PDBe
9B3F contains 101 α-helices and 28 β-strands across 5 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 | 5-10 | 6 | |
| α-helix | 17-28 | 12 | |
| α-helix | 31-45 | 15 | |
| α-helix | 51-65 | 15 | |
| α-helix | 84-99 | 16 | |
| α-helix | 105-121 | 17 | |
| α-helix | 128-140 | 13 | |
| α-helix | 144-156 | 13 | |
| α-helix | 160-164 | 5 | |
| α-helix | 168-181 | 14 | |
| α-helix | 187-206 | 20 | |
| α-helix | 213-235 | 23 | |
| α-helix | 243-263 | 21 | |
| α-helix | 271-290 | 20 | |
| α-helix | 303-320 | 18 | |
| α-helix | 328-342 | 15 | |
| α-helix | 344-345 | 2 | |
| α-helix | 346-354 | 9 | |
| α-helix | 356-363 | 8 | |
| α-helix | 372-381 | 10 | |
| α-helix | 385-402 | 18 | |
| α-helix | 406-408 | 3 | |
| α-helix | 409-420 | 12 | |
| α-helix | 431-447 | 17 | |
| α-helix | 453-469 | 17 | |
| α-helix | 477-494 | 18 | |
| α-helix | 498-514 | 17 | |
| α-helix | 517-521 | 5 | |
| α-helix | 523-540 | 18 | |
| α-helix | 541-543 | 3 | |
| α-helix | 546-562 | 17 | |
| α-helix | 571-587 | 17 | |
| α-helix | 592-606 | 15 | |
| α-helix | 612-614 | 3 | |
| α-helix | 616-620 | 5 | |
| α-helix | 622-634 | 13 | |
| α-helix | 641-656 | 16 | |
| α-helix | 662-664 | 3 | |
| 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 | 728-732 | 5 | |
| α-helix | 734-744 | 11 | |
| α-helix | 750-766 | 17 | |
| α-helix | 770-786 | 17 | |
| α-helix | 788-797 | 10 | |
| β-strand | 799-800 | 2 | 8 |
| β-strand | 803-804 | 2 | 8 |
| α-helix | 805-817 | 13 | |
| α-helix | 823-839 | 17 | |
| α-helix | 842-846 | 5 | |
| β-strand | 848-849 | 2 | 9 |
| β-strand | 853-854 | 2 | 10 |
| α-helix | 855-856 | 2 | |
| α-helix | 864-867 | 4 | |
| β-strand | 873-874 | 2 | 10 |
| β-strand | 877-878 | 2 | 9 |
| α-helix | 879-894 | 16 | |
| α-helix | 933-941 | 9 | |
| α-helix | 965-979 | 15 | |
| α-helix | 981-990 | 10 | |
| α-helix | 993-1003 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 18-22 | 5 | |
| α-helix | 28-38 | 11 | |
| β-strand | 44 | 1 | 11 |
| α-helix | 47-73 | 27 | |
| β-strand | 78-79 | 2 | 12 |
| α-helix | 81-90 | 10 | |
| α-helix | 92-98 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 41-51 | 11 | |
| β-strand | 56-57 | 2 | 12 |
| α-helix | 59-86 | 28 | |
| β-strand | 92 | 1 | 11 |
| α-helix | 94-104 | 11 | |
| α-helix | 107-125 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 82-87 | 6 | |
| α-helix | 90-140 | 51 | |
| α-helix | 147-158 | 12 | |
| α-helix | 163-165 | 3 | |
| α-helix | 167-168 | 2 | |
| α-helix | 169-172 | 4 | |
| α-helix | 176-179 | 4 | |
| α-helix | 188-194 | 7 | |
| α-helix | 197-200 | 4 | |
| α-helix | 205-211 | 7 | |
| β-strand | 216-221 | 6 | 1 |
| β-strand | 228-234 | 7 | 1 |
| β-strand | 243 | 1 | 2 |
| β-strand | 247-254 | 8 | 1 |
| β-strand | 266-271 | 6 | 1 |
| β-strand | 276 | 1 | 2 |
| β-strand | 285-294 | 10 | 3 |
| β-strand | 299-308 | 10 | 3 |
| α-helix | 312-315 | 4 | |
| α-helix | 323-333 | 11 | |
| α-helix | 334-338 | 5 | |
| α-helix | 339-347 | 9 | |
| α-helix | 348-352 | 5 | |
| α-helix | 353-355 | 3 | |
| α-helix | 356-361 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 84-87 | 4 | |
| α-helix | 90-140 | 51 | |
| α-helix | 147-160 | 14 | |
| α-helix | 163-165 | 3 | |
| α-helix | 169-172 | 4 | |
| α-helix | 176-179 | 4 | |
| α-helix | 185 | 1 | |
| α-helix | 188-195 | 8 | |
| α-helix | 199-202 | 4 | |
| α-helix | 205-211 | 7 | |
| β-strand | 214-222 | 9 | 4 |
| β-strand | 228-235 | 8 | 4 |
| β-strand | 243 | 1 | 5 |
| β-strand | 247-254 | 8 | 4 |
| β-strand | 259 | 1 | 6 |
| α-helix | 260-262 | 3 | |
| β-strand | 263 | 1 | 6 |
| α-helix | 264-265 | 2 | |
| β-strand | 266-271 | 6 | 4 |
| β-strand | 276 | 1 | 5 |
| β-strand | 285-293 | 9 | 7 |
| β-strand | 300-308 | 9 | 7 |
| α-helix | 312-315 | 4 | |
| α-helix | 325-327 | 3 | |
| α-helix | 328-347 | 20 | |
| α-helix | 348-352 | 5 | |
| α-helix | 357-361 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NAP1 isoform 1 | D, E | protein | 313 | Saccharomyces cerevisiae | P25293 (AlphaFold model) |
| KAP114 isoform 1 | A | protein | 1007 | Saccharomyces cerevisiae | P53067 (AlphaFold model) |
| Histone H2A | B | protein | 131 | Saccharomyces cerevisiae | P04912 (AlphaFold model) |
| Histone H2B | C | protein | 130 | Saccharomyces cerevisiae | P02294 (AlphaFold model) |
>9B3F_1 NAP1 isoform 1 (chains D, E) MGSSHHHHHHSSGLVPRGSHMLGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKE FQVEMFELENKFLQKYKPIWEQRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEK AQNDSEEEQVKGIPSFWLTALENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLL FRFDSSANPFFTNDILCKTYFYQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQ RNKTTKQVRTIEKITPIESFFNFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKL IPRAVDWFTGAAL
>9B3F_2 KAP114 isoform 1 (chains A) GGSMDINELIIGAQSADKHTREVAETQLLQWCDSDASQVFKALANVALQHEASLESRQFA LLSLRKLITMYWSPGFESYRSTSNVEIDVKDFIREVLLKLCLNDNENTKIKNGASYCIVQ ISAVDFPDQWPQLLTVIYDAISHQHSLNAMSLLNEIYDDVVSEEMFFEGGIGLATMEIVF KVLNTETSTLIAKIAALKLLKACLLQMSSHNEYDEASRKSFVSQCLATSLQILGQLLTLN FGNVDVISQLKFKSIIYENLVFIKNDFSRKHFSSELQKQFKIMAIQDLENVTHINANVET TESEPLLETVHDCSIYIVEFLTSVCTLQFSVEEMNKIITSLTILCQLSSETREIWTSDFN TFVSKETGLAASYNVRDQANEFFTSLPNPQLSLIFKVVSNDIEHSTCNYSTLESLLYLLQ CILLNDDEITGENIDQSLQILIKTLENILVSQEIPELILARAILTIPRVLDKFIDALPDI KPLTSAFLAKSLNLALKSDKELIKSATLIAFTYYCYFAELDSVLGPEVCSETQEKVIRII NQVSSDAEEDTNGALMEVLSQVISYNPKEPHSRKEILQAEFHLVFTISSEDPANVQVVVQ SQECLEKLLDNINMDNYKNYIELCLPSFINVLDSNNANNYRYSPLLSLVLEFITVFLKKK PNDGFLPDEINQYLFEPLAKVLAFSTEDETLQLATEAFSYLIFNTDTRAMEPRLMDIMKV LERLLSLEVSDSAAMNVGPLVVAIFTRFSKEIQPLIGRILEAVVVRLIKTQNISTEQNLL SVLCFLTCNDPKQTVDFLSSFQIDNTDALTLVMRKWIEAFEVIRGEKRIKENIVALSNLF FLNDKRLQKVVVNGNLIPYEGDLIITRSMAKKMPDRYVQVPLYTKIIKLFVSELSFQSKQ PNPEQLITSDIKQEVVNANKDDDNDDWEDVDDVLDYDKLKEYIDDDVDEEADDDSDDITG LMDVKESVVQLLVRFFKEVASKDVSGFHCIYETLSDSERKVLSEALL
>9B3F_3 Histone H2A (chains B) SGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLA AEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKK SAKTAKASQEL
>9B3F_4 Histone H2B (chains C) SSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQK SMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRA VTKYSSSTQA
Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus. Fung, H.Y.J., Jiou, J., Niesman, A.B. et al. J Cell Biol (2025) 224. DOI 10.1083/jcb.202408193 · PubMed
Other PDB entries of the same protein (UniProt P25293 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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