8J91: Histone H3.1

Cryo-EM structure of nucleosome containing Arabidopsis thaliana histones. Determined by electron microscopy at 2.9 Å resolution. Released 3 Jul 2024.

Method
Electron microscopy
Resolution
2.9 Å
Organisms
Arabidopsis thaliana, synthetic construct
Chains
10
Atoms
9,944
Mol. weight
220.77 kDa
Released
3 Jul 2024

Explore 8J91 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8J91 contains 33 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.

Chain A: 3 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix64-7613
β-strand83-8421
α-helix86-11328
β-strand118-11922
α-helix121-13111
Chains B and F: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4010
β-strand45-4622
α-helix50-7526
β-strand80-8121
α-helix83-9210
β-strand97-9823
Chain C: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix18-225
α-helix28-369
β-strand43-4424
α-helix49-524
α-helix58-7316
β-strand78-7925
α-helix81-9010
α-helix92-987
β-strand102-10326
Chain D: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix64-7310
β-strand78-7925
α-helix81-10727
β-strand113-11424
α-helix116-12611
α-helix129-14820
Chain E: 3 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix64-7512
β-strand83-8427
α-helix86-11328
β-strand118-11928
α-helix121-13111
Chain G: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix18-225
α-helix28-3710
β-strand43-4429
α-helix49-7325
β-strand78-79210
α-helix81-877
α-helix92-987
β-strand102-10323
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix63-7311
β-strand78-79210
α-helix81-10828
β-strand113-11429
α-helix116-12611
α-helix129-14820

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3.1A, Eprotein139Arabidopsis thalianaP59226 (AlphaFold model)
Histone H4B, Fprotein106Arabidopsis thalianaP59259 (AlphaFold model)
HTA13C, Gprotein135Arabidopsis thalianaQ9LHQ5 (AlphaFold model)
Histone H2B.6D, Hprotein153Arabidopsis thalianaO23629 (AlphaFold model)
DNA (169-mer)IDNA169synthetic construct
DNA (169-mer)JDNA169synthetic construct
Sequence of entity 1 (A, E), FASTA
>8J91_1 Histone H3.1 (chains A, E)
GSHMARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQK
STELLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKR
VTIMPKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>8J91_2 Histone H4 (chains B, F)
GSHMSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRG
VLKIFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>8J91_3 HTA13 (chains C, G)
GSHMAGRGKTLGSGVAKKSTSRSSKAGLQFPVGRIARFLKNGKYATRVGAGAPVYLAAVL
EYLAAEVLELAGNAARDNKKTRIVPRHIQLAVRNDEELSKLLGDVTIANGGVMPNIHSLL
LPKKAGASKPSADED
Sequence of entity 4 (D, H), FASTA
>8J91_4 Histone H2B.6 (chains D, H)
GSHMAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKK
KSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITS
REIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
Sequence of entity 5 (I), FASTA
>8J91_5 DNA (169-MER) (chains I)
ATCGGACCCTATCGCGAGCCAGGCCTGAGAATCCGGTGCCGAGGCCGCTCAATTGGTCGT
AGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAA
GGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCGAT
Sequence of entity 6 (J), FASTA
>8J91_6 DNA (169-MER) (chains J)
ATCGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAA
AACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTG
AGCGGCCTCGGCACCGGATTCTCAGGCCTGGCTCGCGATAGGGTCCGAT

Primary citation

Molecular and structural basis of the chromatin remodeling activity by Arabidopsis DDM1. Osakabe, A., Takizawa, Y., Horikoshi, N. et al. Nat Commun (2024) 15:5187-5187. DOI 10.1038/s41467-024-49465-w · PubMed

Other PDB entries of the same protein (UniProt P59226 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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