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; PubMed: 21454705; DOI: 10.1074/jbc.C111.220715

Experimental method

X-RAY DIFFRACTION (2.705 Å)