5E74
Crystal Structure of BAZ2B bromodomain in complex with acetylindole compound UZH50
Summary for 5E74
| Entry DOI | 10.2210/pdb5e74/pdb |
| Related | 5E73 |
| Descriptor | Bromodomain adjacent to zinc finger domain protein 2B, N-(1-acetyl-1H-indol-3-yl)-N-(5-hydroxy-2-methylphenyl)-3-(trifluoromethyl)benzamide (3 entities in total) |
| Functional Keywords | four helical bundle, transcription |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus : Q9UIF8 |
| Total number of polymer chains | 1 |
| Total formula weight | 13984.00 |
| Authors | Lolli, G.,Spiliotopoulos, D.,Dolbois, A.,Nevado, C.,Caflisch, A. (deposition date: 2015-10-11, release date: 2015-10-21, Last modification date: 2024-01-10) |
| Primary citation | Unzue, A.,Zhao, H.,Lolli, G.,Dong, J.,Zhu, J.,Zechner, M.,Dolbois, A.,Caflisch, A.,Nevado, C. The "Gatekeeper" Residue Influences the Mode of Binding of Acetyl Indoles to Bromodomains. J. Med. Chem., 59:3087-3097, 2016 Cited by PubMed Abstract: Small-molecule hits for the bromodomains of CREBBP and BAZ2B have been identified by scaffold hopping followed by docking of a set of ∼200 compounds containing the acetyl indole scaffold. Chemical synthesis of nearly 30 derivatives has resulted in ligands of representatives of three subfamilies of human bromodomains with favorable ligand efficiency. The X-ray crystal structures of three different bromodomains (CREBBP, BAZ2B, and BRPF1b) in complex with acetyl indole derivatives reveal the influence of the gatekeeper residue on the orientation of small-molecule ligands in the acetyl lysine binding site. PubMed: 26982797DOI: 10.1021/acs.jmedchem.5b01757 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.783 Å) |
Structure validation
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