4A7J
Symmetric Dimethylation of H3 Arginine 2 is a Novel Histone Mark that Supports Euchromatin Maintenance
Summary for 4A7J
Entry DOI | 10.2210/pdb4a7j/pdb |
Related | 2CNX 2CO0 2G99 2G9A 2GNQ 2H13 2H14 2H68 2H6K 2H6N 2H6Q 2V1D 2YBP 2YBS |
Descriptor | WD REPEAT-CONTAINING PROTEIN 5, HISTONE H3.1T (3 entities in total) |
Functional Keywords | transcription, histone methylation |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus: P61964 Q16695 |
Total number of polymer chains | 2 |
Total formula weight | 36526.49 |
Authors | Migliori, V.,Muller, J.,Phalke, S.,Low, D.,Bezzi, M.,ChuenMok, W.,Gunaratne, J.,Capasso, P.,Bassi, C.,Cecatiello, V.,DeMarco, A.,Blackstock, W.,Kuznetsov, V.,Amati, B.,Mapelli, M.,Guccione, E. (deposition date: 2011-11-14, release date: 2012-01-11, Last modification date: 2023-12-20) |
Primary citation | Migliori, V.,Muller, J.,Phalke, S.,Low, D.,Bezzi, M.,Chuenmok, W.,Sahu, S.K.,Gunaratne, J.,Capasso, P.,Bassi, C.,Cecatiello, V.,Demarco, A.,Blackstock, W.,Kuznetsov, V.,Amati, B.,Mapelli, M.,Guccione, E. Symmetric Dimethylation of H3R2 is a Newly Identified Histone Mark that Supports Euchromatin Maintenance Nat.Struct.Mol.Biol., 19:136-, 2012 Cited by PubMed: 22231400DOI: 10.1038/NSMB.2209 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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