8G8G: Histone H3

Interaction of H3 tail in LIN28B nucleosome with Oct4. Determined by electron microscopy at 3.2 Å resolution. Released 22 Mar 2023.

Method
Electron microscopy
Resolution
3.2 Å
Organisms
Xenopus laevis, Homo sapiens
Chains
11
Atoms
14,558
Mol. weight
262.79 kDa
Released
22 Mar 2023

Explore 8G8G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G8G contains 47 α-helices and 20 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.

Chains A and E: 4 helices, 2 β-strands

ElementResiduesLengthSheet
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-strand96-9833
Chain C: 6 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix12-143
α-helix17-215
α-helix27-3610
β-strand42-4324
α-helix46-7227
β-strand77-7825
α-helix80-8910
α-helix91-966
β-strand100-10236
Chain D: 5 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix28-303
α-helix35-4511
β-strand50-5125
α-helix53-8028
β-strand85-8624
α-helix88-9811
α-helix102-12120
Chain F: 4 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix26-283
α-helix31-4010
β-strand45-4628
α-helix50-7526
β-strand80-8127
α-helix83-9210
β-strand96-9836
Chain G: 8 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix12-143
α-helix17-215
α-helix27-359
β-strand42-4329
α-helix46-7227
β-strand77-78210
α-helix80-8910
α-helix91-966
β-strand100-10233
α-helix113-1153
α-helix117-1193
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix35-4511
β-strand50-51210
α-helix53-8028
β-strand85-8629
α-helix88-9811
α-helix102-12120
Chain X: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix142-16019
α-helix164-17512
α-helix181-1888
α-helix194-21017
α-helix216-2194
α-helix239-24810
α-helix257-26711
α-helix271-28717

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone H3A, Eprotein135Xenopus laevisP84233 (AlphaFold model)
Histone H4B, Fprotein102Xenopus laevisP62799 (AlphaFold model)
Histone H2AC, Gprotein129Xenopus laevisQ6AZJ8 (AlphaFold model)
Histone H2BD, Hprotein122Xenopus laevisP02281 (AlphaFold model)
LIN28B DNA (174-mer)IDNA182Homo sapiens
LIN28B DNA (174-mer)JDNA182Homo sapiens
POU domain, class 5, transcription factor 1Xprotein395Homo sapiensQ01860
Sequence of entity 1 (A, E), FASTA
>8G8G_1 Histone H3 (chains A, E)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA
Sequence of entity 2 (B, F), FASTA
>8G8G_2 Histone H4 (chains B, F)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Sequence of entity 3 (C, G), FASTA
>8G8G_3 Histone H2A (chains C, G)
SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTA
EILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKT
ESSKSAKSK
Sequence of entity 4 (D, H), FASTA
>8G8G_4 Histone H2B (chains D, H)
AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMN
SFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTS
AK
Sequence of entity 5 (I), FASTA
>8G8G_5 LIN28B DNA (174-MER) (chains I)
ATGAAGTATGTGTCTTTATTCACAAGCTTGCACAATCCCTGCTGGACAATTCTGAGTGAT
GGCAGCTCCCACCTTTCCTTCTTTCTTCACTTAGACTACATTTATTCAGCATCTGTATTG
TTGGAGTAAGTTCCATGTTAATACTCACCACTGAGGATATGTTAATACCACTTAACTTAT
GC
Sequence of entity 6 (J), FASTA
>8G8G_6 LIN28B DNA (174-MER) (chains J)
GCATAAGTTAAGTGGTATTAACATATCCTCAGTGGTGAGTATTAACATGGAACTTACTCC
AACAATACAGATGCTGAATAAATGTAGTCTAAGTGAAGAAAGAAGGAAAGGTGGGAGCTG
CCATCACTCAGAATTGTCCAGCAGGGATTGTGCAAGCTTGTGAATAAAGACACATACTTC
AT
Sequence of entity 7 (X), FASTA
>8G8G_7 POU domain, class 5, transcription factor 1 (chains X)
GSSHHHHHHSSGLVPRGSHMASMTGGQQMGRDPNSMAGHLASDFAFSPPPGGGGDGPGGP
EPGWVDPRTWLSFQGPPGGPGIGPGVGPGSEVWGIPPCPPPYEFCGGMAYCGPQVGVGLV
PQGGLETSQPEGEAGVGVESNSDGASPEPCTVTPGAVKLEKEKLEQNPEESQDIKALQKE
LEQFAKLLKQKRITLGYTQADVGLTLGVLFGKVFSQTTICRFEALQLSFKNMCKLRPLLQ
KWVEEADNNENLQEICKAETLVQARKRKRTSIENRVRGNLENLFLQCPKPTLQQISHIAQ
QLGLEKDVVRVWFCNRRQKGKRSSSDYAQREDFEAAGSPFSGGPVSFPLAPGPHFGTPGY
GSPHFTALYSSVPFPEGEAFPPVSVTTLGSPMHSN

Primary citation

Histone modifications regulate pioneer transcription factor cooperativity. Sinha, K.K., Bilokapic, S., Du, Y. et al. Nature (2023) 619:378-384. DOI 10.1038/s41586-023-06112-6 · 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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