8G8E: Human Oct4

Human Oct4 bound to nucleosome with human LIN28B sequence. Determined by electron microscopy at 3.9 Å resolution. Released 22 Mar 2023.

Method
Electron microscopy
Resolution
3.9 Å
Organism
Homo sapiens
Chains
3
Atoms
2,464
Mol. weight
154.65 kDa
Released
22 Mar 2023

Explore 8G8E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G8E contains 8 α-helices and 0 β-strands across 1 chain. 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 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
LIN28B DNA (32-mer)JDNA182Homo sapiens
LIN28B DNA (32-mer)IDNA182Homo sapiens
POU domain, class 5, transcription factor 1Xprotein395Homo sapiensQ01860 (AlphaFold model)
Sequence of entity 1 (J), FASTA
>8G8E_1 LIN28B DNA (32-MER) (chains J)
GCATAAGTTAAGTGGTATTAACATATCCTCAGTGGTGAGTATTAACATGGAACTTACTCC
AACAATACAGATGCTGAATAAATGTAGTCTAAGTGAAGAAAGAAGGAAAGGTGGGAGCTG
CCATCACTCAGAATTGTCCAGCAGGGATTGTGCAAGCTTGTGAATAAAGACACATACTTC
AT
Sequence of entity 2 (I), FASTA
>8G8E_2 LIN28B DNA (32-MER) (chains I)
ATGAAGTATGTGTCTTTATTCACAAGCTTGCACAATCCCTGCTGGACAATTCTGAGTGAT
GGCAGCTCCCACCTTTCCTTCTTTCTTCACTTAGACTACATTTATTCAGCATCTGTATTG
TTGGAGTAAGTTCCATGTTAATACTCACCACTGAGGATATGTTAATACCACTTAACTTAT
GC
Sequence of entity 3 (X), FASTA
>8G8E_3 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 Q01860 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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