9K3Z: Histone H3.1

Cryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry). Determined by electron microscopy at 2.75 Å resolution. Released 14 May 2025.

Method
Electron microscopy
Resolution
2.75 Å
Organism
Arabidopsis thaliana
Chains
10
Atoms
11,814
Mol. weight
205.68 kDa
Released
14 May 2025

Explore 9K3Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9K3Z contains 40 α-helices and 22 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.

Chains A and E: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix41-422
α-helix45-5612
α-helix64-7512
β-strand83-8421
α-helix86-11328
β-strand118-11922
α-helix121-13111
Chain B: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix25-284
α-helix31-4010
β-strand45-4622
α-helix50-7526
β-strand80-8121
α-helix83-9210
β-strand97-9823
Chain C: 6 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix28-314
α-helix38-4811
β-strand5014
β-strand54-5525
α-helix57-8428
β-strand89-9026
α-helix92-1009
α-helix103-1086
β-strand112-11327
α-helix124-1263
Chain D: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix56-583
α-helix61-7111
β-strand76-7726
α-helix79-10628
β-strand111-11225
α-helix114-12411
α-helix127-14620
Chain F: 5 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4010
β-strand45-4629
α-helix50-7526
β-strand80-8128
α-helix821
α-helix83-9210
β-strand97-9827
Chain G: 6 helices, 4 β-strands
ElementResiduesLengthSheet
α-helix28-314
α-helix38-4811
β-strand5014
β-strand54-55210
α-helix57-8428
β-strand89-90211
α-helix92-10110
α-helix103-1086
β-strand112-11323
α-helix124-1263
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix61-7111
β-strand76-77211
α-helix79-10628
β-strand111-112210
α-helix114-12411
α-helix127-14620

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3.1A, Eprotein136Arabidopsis thalianaP59226 (AlphaFold model)
Histone H4B, Fprotein103Arabidopsis thalianaP59259 (AlphaFold model)
Probable histone H2A variant 3C, Gprotein134Arabidopsis thalianaQ9C944 (AlphaFold model)
Histone H2B.1D, Hprotein148Arabidopsis thalianaQ9LQQ4 (AlphaFold model)
15.2.2 DNA (147-mer)IDNA147Arabidopsis thaliana
15.2.2 DNA (147-mer)JDNA147Arabidopsis thaliana
Sequence of entity 1 (A, E), FASTA
>9K3Z_1 Histone H3.1 (chains A, E)
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTE
LLIRKLPFQRLVREIAQDFKTDLRFQSSAVAALQEAAEAYLVGLFEDTNLCAIHAKRVTI
MPKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>9K3Z_2 Histone H4 (chains B, F)
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK
IFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>9K3Z_3 Probable histone H2A variant 3 (chains C, G)
MSGKGAKGLIMGKPSGSDKDKDKKKPITRSSRAGLQFPVGRVHRLLKTRSTAHGRVGATA
AVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELDTLIKGTIAGGGVI
PHIHKSLINKSAKE
Sequence of entity 4 (D, H), FASTA
>9K3Z_4 Histone H2B.1 (chains D, H)
MAPRAEKKPAEKKTAAERPVEENKAAEKAPAEKKPKAGKKLPPKEAGDKKKKRSKKNVET
YKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKKPTITSREIQT
AVRLVLPGELAKHAVSEGTKAVTKFTSS
Sequence of entity 5 (I), FASTA
>9K3Z_5 15.2.2 DNA (147-MER) (chains I)
ACCTTTATTGACTCCATAATTGACCAATTGAGCGGCTCGATTCAACTGTCAATAACTTCA
AATGAAGCAAGAGCCTTATCGTATTCTCCGCACGATGGTGCTTTAATCCACCGCAACTTT
CCTCTTTAATAAAGGCACAAGCATTAA
Sequence of entity 6 (J), FASTA
>9K3Z_6 15.2.2 DNA (147-MER) (chains J)
TTAATGCTTGTGCCTTTATTAAAGAGGAAAGTTGCGGTGGATTAAAGCACCATCGTGCGG
AGAATACGATAAGGCTCTTGCTTCATTTGAAGTTATTGACAGTTGAATCGAGCCGCTCAA
TTGGTCAATTATGGAGTCAATAAAGGT

Primary citation

Structural and functional interrelationships of histone H2A with its variants H2A.Z and H2A.W in Arabidopsis. Wang, Y., Wu, J., Yang, S. et al. Structure (2025) 33:1240. DOI 10.1016/j.str.2025.04.015 · PubMed

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

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