3Q66
Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P6122)
Summary for 3Q66
Entry DOI | 10.2210/pdb3q66/pdb |
Related | 3Q68 |
Descriptor | Vacuolar protein sorting-associated protein 75, Histone acetyltransferase RTT109, SULFATE ION, ... (4 entities in total) |
Functional Keywords | histone chaperone, lysine acetyltransferase, chaperone-transferase complex, chaperone/transferase |
Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) More |
Cellular location | Nucleus: P53853 Q07794 |
Total number of polymer chains | 3 |
Total formula weight | 112310.76 |
Authors | Su, D.,Thompson, J.R.,Mer, G. (deposition date: 2010-12-30, release date: 2011-03-23, Last modification date: 2023-12-06) |
Primary citation | Su, D.,Hu, Q.,Zhou, H.,Thompson, J.R.,Xu, R.M.,Zhang, Z.,Mer, G. Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. J.Biol.Chem., 286:15625-15629, 2011 Cited by PubMed: 21454705DOI: 10.1074/jbc.C111.220715 PDB entries with the same primary citation |
Experimental method |
Structure validation
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