8G87: Human Oct4

Human Oct4 bound to nucleosome with human nMatn1 sequence (focused refinement of Oct4 bound region). Determined by electron microscopy at 8.1 Å resolution. Released 22 Mar 2023.

Method
Electron microscopy
Resolution
8.1 Å
Organism
Homo sapiens
Chains
3
Atoms
1,777
Mol. weight
157.12 kDa
Released
22 Mar 2023

Explore 8G87 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8G87 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
nMatn1 DNA (top strand)IDNA186Homo sapiens
nMatn1 DNA (bottom strand)JDNA186Homo sapiens
POU domain, class 5, transcription factor 1Xprotein395Homo sapiensQ01860 (AlphaFold model)
Sequence of entity 1 (I), FASTA
>8G87_1 nMatn1 DNA (top strand) (chains I)
ACATGCACACATGCTAATATATGCACACAATGCACACAGGTTAATATATACACATACACA
CACATGCACACACACGTGCACACATATATGCACATGCATGCACACACGTATATGCACACA
CATGCACATGCATGCGCACATAGTCACACACATGCACACATTAGCATATGCATACACATA
CATGCA
Sequence of entity 2 (J), FASTA
>8G87_2 nMatn1 DNA (bottom strand) (chains J)
TGCATGTATGTGTATGCATATGCTAATGTGTGCATGTGTGTGACTATGTGCGCATGCATG
TGCATGTGTGTGCATATACGTGTGTGCATGCATGTGCATATATGTGTGCACGTGTGTGTG
CATGTGTGTGTATGTGTATATATTAACCTGTGTGCATTGTGTGCATATATTAGCATGTGT
GCATGT
Sequence of entity 3 (X), FASTA
>8G87_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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