Cryo-EM structure of Arabidopsis thaliana H2A.Z-H3.3-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry). Determined by electron microscopy at 2.71 Å resolution. Released 12 Nov 2025.
Explore 9K45 in 3D Show helices and sheets RCSB PDB PDBe
9K45 contains 36 α-helices and 20 β-strands across 8 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 | 45-54 | 10 | |
| α-helix | 64-75 | 12 | |
| β-strand | 83-84 | 2 | 1 |
| α-helix | 86-113 | 28 | |
| β-strand | 118-119 | 2 | 2 |
| α-helix | 121-131 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-28 | 3 | |
| α-helix | 31-40 | 10 | |
| β-strand | 45-46 | 2 | 2 |
| α-helix | 50-75 | 26 | |
| β-strand | 80-81 | 2 | 1 |
| α-helix | 83-92 | 10 | |
| β-strand | 97-98 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-32 | 5 | |
| α-helix | 38-48 | 11 | |
| β-strand | 54-55 | 2 | 4 |
| α-helix | 57-84 | 28 | |
| β-strand | 89-90 | 2 | 5 |
| α-helix | 92-100 | 9 | |
| α-helix | 103-108 | 6 | |
| α-helix | 111 | 1 | |
| β-strand | 112-113 | 2 | 6 |
| α-helix | 124-126 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-71 | 11 | |
| β-strand | 76-77 | 2 | 5 |
| α-helix | 79-106 | 28 | |
| β-strand | 111-112 | 2 | 4 |
| α-helix | 114-124 | 11 | |
| α-helix | 127-146 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-32 | 5 | |
| α-helix | 38-48 | 11 | |
| β-strand | 54-55 | 2 | 9 |
| α-helix | 57-84 | 28 | |
| β-strand | 89-90 | 2 | 10 |
| α-helix | 92-100 | 9 | |
| α-helix | 103-108 | 6 | |
| β-strand | 112-113 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H3.3 | A, E | protein | 136 | Arabidopsis thaliana | P59169 (AlphaFold model) |
| Histone H4 | B, F | protein | 103 | Arabidopsis thaliana | P59259 (AlphaFold model) |
| Probable histone H2A variant 3 | C, G | protein | 134 | Arabidopsis thaliana | Q9C944 (AlphaFold model) |
| Histone H2B.1 | D, H | protein | 148 | Arabidopsis thaliana | Q9LQQ4 (AlphaFold model) |
| 15.2.2 DNA (147-mer) | I | DNA | 147 | Arabidopsis thaliana | |
| 15.2.2 DNA (147-mer) | J | DNA | 147 | Arabidopsis thaliana |
>9K45_1 Histone H3.3 (chains A, E) MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTE LLIRKLPFQRLVREIAQDFKTDLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTI MPKDIQLARRIRGERA
>9K45_2 Histone H4 (chains B, F) MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK IFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
>9K45_3 Probable histone H2A variant 3 (chains C, G) MSGKGAKGLIMGKPSGSDKDKDKKKPITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATA AVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELDTLIKGTIAGGGVI PHIHKSLINKSAKE
>9K45_4 Histone H2B.1 (chains D, H) MAPRAEKKPAEKKTAAERPVEENKAAEKAPAEKKPKAGKKLPPKEAGDKKKKRSKKNVET YKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKKPTITSREIQT AVRLVLPGELAKHAVSEGTKAVTKFTSS
>9K45_5 15.2.2 DNA (147-MER) (chains I) ACCTTTATTGACTCCATAATTGACCAATTGAGCGGCTCGATTCAACTGTCAATAACTTCA AATGAAGCAAGAGCCTTATCGTATTCTCCGCACGATGGTGCTTTAATCCACCGCAACTTT CCTCTTTAATAAAGGCACAAGCATTAA
>9K45_6 15.2.2 DNA (147-MER) (chains J) TTAATGCTTGTGCCTTTATTAAAGAGGAAAGTTGCGGTGGATTAAAGCACCATCGTGCGG AGAATACGATAAGGCTCTTGCTTCATTTGAAGTTATTGACAGTTGAATCGAGCCGCTCAA TTGGTCAATTATGGAGTCAATAAAGGT
Functional redundancy of core histone H2A and its variants in Arabidopsis. Wang, Y., Dong, A. To be published.
Other PDB entries of the same protein (UniProt P59169 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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