8IHM: Eaf3 CHD domain

Eaf3 CHD domain bound to the nucleosome. Determined by electron microscopy at 3.58 Å resolution. Released 20 Mar 2024.

Method
Electron microscopy
Resolution
3.58 Å
Organisms
Xenopus laevis, Saccharomyces cerevisiae
Chains
12
Atoms
13,153
Mol. weight
225.81 kDa
Released
20 Mar 2024

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

Secondary structure: helices and β-sheets

8IHM contains 42 α-helices and 28 β-strands across 9 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix41-422
α-helix45-528
α-helix64-7613
β-strand83-8421
α-helix86-11429
β-strand11912
α-helix121-1299
Chain B: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4111
β-strand4612
α-helix50-7627
β-strand80-8121
α-helix83-9210
β-strand97-9823
Chain C: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-204
α-helix27-3610
β-strand42-4324
α-helix46-7025
α-helix71-733
β-strand7815
α-helix80-8910
α-helix91-966
β-strand101-10226
Chain D: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand5115
α-helix53-7321
α-helix76-805
β-strand85-8624
α-helix89-9810
α-helix102-12120
Chain E: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix40-423
α-helix47-548
α-helix64-7815
β-strand83-8427
α-helix86-11328
β-strand11918
α-helix121-13010
Chain F: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4111
β-strand4618
α-helix49-7527
β-strand80-8127
α-helix83-9311
β-strand97-9826
Chain G: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix17-204
α-helix27-3610
β-strand42-4329
α-helix46-7328
β-strand77-78210
α-helix80-8910
α-helix91-944
α-helix95-973
β-strand101-10223
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand50-51210
α-helix55-8026
β-strand85-8629
α-helix88-9811
α-helix102-12019

1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3A, Eprotein135Xenopus laevisP84233 (AlphaFold model)
Histone H4B, Fprotein102Xenopus laevisP62799 (AlphaFold model)
Histone H2AC, Gprotein129Xenopus laevisP06897 (AlphaFold model)
Histone H2BD, Hprotein122Xenopus laevisP02281 (AlphaFold model)
DNA (164-mer)IDNA164Xenopus laevis
DNA (165-mer)JDNA165Xenopus laevis
Rco1-ABRMprotein18Saccharomyces cerevisiaeQ04779
Chromatin modification-related protein EAF3Nprotein119Saccharomyces cerevisiaeQ12432
Sequence of entity 1 (A, E), FASTA
>8IHM_1 Histone H3 (chains A, E)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLAAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>8IHM_2 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>8IHM_3 Histone H2A (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 4 (D, H), FASTA
>8IHM_4 Histone H2B (chains D, H)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 5 (I), FASTA
>8IHM_5 DNA (164-MER) (chains I)
TCGCCCTTACTGGCCGCCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGAC
AGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGG
ATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTG
Sequence of entity 6 (J), FASTA
>8IHM_6 DNA (165-MER) (chains J)
CAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCTTGGCGGTTAAA
ACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTACGACCAATTGA
GCGGCCTCGGCACCGGGATTCTCCAGGGCGGCCAGTAAGGGCGAC
Sequence of entity 7 (M), FASTA
>8IHM_7 Rco1-ABR (chains M)
RRKIITSEGIERSFKNEH
Sequence of entity 8 (N), FASTA
>8IHM_8 Chromatin modification-related protein EAF3 (chains N)
RCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQKLGEDESIPEEII
NGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKKSLLEQQKKKKL

Primary citation

Structural basis for nucleosome binding and catalysis by the yeast Rpd3S/HDAC holoenzyme. Zhang, Y., Xu, M., Wang, P. et al. Cell Res (2023) 33:971-974. DOI 10.1038/s41422-023-00884-2 · PubMed

Other PDB entries of the same protein (UniProt P84233 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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