3G7L
Chromodomain of Chp1 in complex with Histone H3K9me3 peptide
Summary for 3G7L
Entry DOI | 10.2210/pdb3g7l/pdb |
Descriptor | Chromo domain-containing protein 1, Histone H3.1/H3.2, ACETIC ACID, ... (5 entities in total) |
Functional Keywords | chromodomain, 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 source | Schizosaccharomyces pombe (Fission yeast) More |
Cellular location | Nucleus: Q10103 Nucleus (By similarity): P09988 |
Total number of polymer chains | 2 |
Total formula weight | 9475.92 |
Authors | Schalch, T.,Joshua-Tor, L. (deposition date: 2009-02-10, release date: 2009-04-21, Last modification date: 2023-09-06) |
Primary citation | Schalch, 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: 19362535DOI: 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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