3Q33
Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation
Summary for 3Q33
Entry DOI | 10.2210/pdb3q33/pdb |
Related | 3D35 3DM7 3Q35 |
Descriptor | Histone acetyltransferase RTT109, Vacuolar protein sorting-associated protein 75, HISTONE H3, ... (6 entities in total) |
Functional Keywords | rtt109:vps75=2:2 stoichiometry complex, histone acetyltransferase, with acetyl coenzyme a (acoa) bound, autoacetylation on rtt109 lys290, nuclear, transferase-chaperone-transcription regulator complex, transferase-chaperone complex, transferase, chaperone-gene regulation complex, chaperone/gene regulation |
Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) More |
Cellular location | Nucleus: Q07794 P53853 P61830 |
Total number of polymer chains | 3 |
Total formula weight | 80005.95 |
Authors | Tang, Y.,Yuan, H.,Meeth, K.,Marmorstein, R. (deposition date: 2010-12-21, release date: 2011-02-02, Last modification date: 2023-12-06) |
Primary citation | Tang, Y.,Holbert, M.A.,Delgoshaie, N.,Wurtele, H.,Guillemette, B.,Meeth, K.,Yuan, H.,Drogaris, P.,Lee, E.H.,Durette, C.,Thibault, P.,Verreault, A.,Cole, P.A.,Marmorstein, R. Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation. Structure, 19:221-231, 2011 Cited by PubMed: 21256037DOI: 10.1016/j.str.2010.12.012 PDB entries with the same primary citation |
Experimental method |
Structure validation
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