3BIY
Crystal structure of p300 histone acetyltransferase domain in complex with a bisubstrate inhibitor, Lys-CoA
Summary for 3BIY
Entry DOI | 10.2210/pdb3biy/pdb |
Descriptor | Histone acetyltransferase p300, BROMIDE ION, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R,20R)-20-carbamoyl-3-hydroxy-2,2-dimethyl-4,8,14,22-tetraoxo-12-thia-5,9,15,21-tetraazatricos-1-yl dihydrogen diphosphate, ... (4 entities in total) |
Functional Keywords | p300 hat, bisubstrate inhibitor, protein-inhibitor complex, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: Q09472 |
Total number of polymer chains | 1 |
Total formula weight | 45370.24 |
Authors | Liu, X.,Wang, L.,Zhao, K.,Thompson, P.R.,Hwang, Y.,Marmorstein, R.,Cole, P.A. (deposition date: 2007-12-02, release date: 2008-02-12, Last modification date: 2024-02-21) |
Primary citation | Liu, X.,Wang, L.,Zhao, K.,Thompson, P.R.,Hwang, Y.,Marmorstein, R.,Cole, P.A. The structural basis of protein acetylation by the p300/CBP transcriptional coactivator Nature, 451:846-850, 2008 Cited by PubMed: 18273021DOI: 10.1038/nature06546 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report