5FE4
Crystal structure of human PCAF bromodomain in complex with fragment MB364 (fragment 5)
Summary for 5FE4
| Entry DOI | 10.2210/pdb5fe4/pdb |
| Descriptor | Histone acetyltransferase KAT2B, 1,2-ETHANEDIOL, 2,3-dihydro-1,4-benzodioxine-5-carboxamide, ... (4 entities in total) |
| Functional Keywords | signaling protein, bromodomain, histone acetyltransferase kat2b, histone, acetylation, acetyllysine, epigenetics, structural genomics consortium (sgc) |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus : Q92831 |
| Total number of polymer chains | 2 |
| Total formula weight | 29013.43 |
| Authors | Chaikuad, A.,von Delft, F.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Knapp, S.,Structural Genomics Consortium (SGC) (deposition date: 2015-12-16, release date: 2016-01-13, Last modification date: 2024-01-10) |
| Primary citation | Chaikuad, A.,Lang, S.,Brennan, P.E.,Temperini, C.,Fedorov, O.,Hollander, J.,Nachane, R.,Abell, C.,Muller, S.,Siegal, G.,Knapp, S. Structure-Based Identification of Inhibitory Fragments Targeting the p300/CBP-Associated Factor Bromodomain. J.Med.Chem., 59:1648-1653, 2016 Cited by PubMed Abstract: The P300/CBP-associated factor plays a central role in retroviral infection and cancer development, and the C-terminal bromodomain provides an opportunity for selective targeting. Here, we report several new classes of acetyl-lysine mimetic ligands ranging from mM to low micromolar affinity that were identified using fragment screening approaches. The binding modes of the most attractive fragments were determined using high resolution crystal structures providing chemical starting points and structural models for the development of potent and selective PCAF inhibitors. PubMed: 26731131DOI: 10.1021/acs.jmedchem.5b01719 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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