Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4PCE

Crystal Structure of the first bromodomain of human BRD4 in complex with compound B13

Summary for 4PCE
Entry DOI10.2210/pdb4pce/pdb
Related4PCI
DescriptorBromodomain-containing protein 4, 1,2-ETHANEDIOL, 1-benzyl-2-ethyl-1,5,6,7-tetrahydro-4H-indol-4-one, ... (4 entities in total)
Functional Keywordstranscription-transcription inhibitor complex, transcription/transcription inhibitor
Biological sourceHomo sapiens (Human)
Cellular locationNucleus: O60885
Total number of polymer chains1
Total formula weight15414.79
Authors
Dong, J.,Caflisch, A. (deposition date: 2014-04-15, release date: 2014-05-07, Last modification date: 2023-12-27)
Primary citationZhao, H.,Gartenmann, L.,Dong, J.,Spiliotopoulos, D.,Caflisch, A.
Discovery of BRD4 bromodomain inhibitors by fragment-based high-throughput docking.
Bioorg.Med.Chem.Lett., 24:2493-2496, 2014
Cited by
PubMed Abstract: Bromodomains (BRDs) recognize acetyl-lysine modified histone tails mediating epigenetic processes. BRD4, a protein containing two bromodomains, has emerged as an attractive therapeutic target for several types of cancer as well as inflammatory diseases. Using a fragment-based in silico screening approach, we identified two small molecules that bind to the first bromodomain of BRD4 with low-micromolar affinity and favorable ligand efficiency (0.37 kcal/mol per non-hydrogen atom), selectively over other families of bromodomains. Notably, the hit rate of the fragment-based in silico approach is about 10% as only 24 putative inhibitors, from an initial library of about 9 million molecules, were tested in vitro.
PubMed: 24767840
DOI: 10.1016/j.bmcl.2014.04.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.293 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon