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3G7L

Chromodomain of Chp1 in complex with Histone H3K9me3 peptide

Summary for 3G7L
Entry DOI10.2210/pdb3g7l/pdb
DescriptorChromo domain-containing protein 1, Histone H3.1/H3.2, ACETIC ACID, ... (5 entities in total)
Functional Keywordschromodomain, protein-peptide complex, silencing, cell cycle, chromosome partition, dna-binding, nucleus, rna-mediated gene silencing, acetylation, chromosomal protein, dna damage, dna repair, methylation, nucleosome core, phosphoprotein, nuclear protein
Biological sourceSchizosaccharomyces pombe (Fission yeast)
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Cellular locationNucleus: Q10103
Nucleus (By similarity): P09988
Total number of polymer chains2
Total formula weight9475.92
Authors
Schalch, T.,Joshua-Tor, L. (deposition date: 2009-02-10, release date: 2009-04-21, Last modification date: 2023-09-06)
Primary citationSchalch, T.,Job, G.,Noffsinger, V.J.,Shanker, S.,Kuscu, C.,Joshua-Tor, L.,Partridge, J.F.
High-affinity binding of Chp1 chromodomain to K9 methylated histone H3 is required to establish centromeric heterochromatin
Mol.Cell, 34:36-46, 2009
Cited by
PubMed: 19362535
DOI: 10.1016/j.molcel.2009.02.024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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