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; PubMed: 18273021; DOI: 10.1038/nature06546

Experimental method

X-RAY DIFFRACTION (1.7 Å)