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6FR0

Crystal structure of CREBBP bromodomain complexd with PB08

Summary for 6FR0
Entry DOI10.2210/pdb6fr0/pdb
DescriptorCREB-binding protein, ~{N}-[3-(5-ethanoyl-2-ethoxy-phenyl)-5-(2-ethyl-5-methyl-3-oxidanylidene-1,2-oxazol-4-yl)phenyl]furan-2-carboxamide (3 entities in total)
Functional Keywordsinhibitor, bromodomain, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight29395.71
Authors
Zhu, J.,Caflisch, A. (deposition date: 2018-02-15, release date: 2018-08-29, Last modification date: 2024-01-17)
Primary citationZhu, J.,Dong, J.,Batiste, L.,Unzue, A.,Dolbois, A.,Pascanu, V.,Sledz, P.,Nevado, C.,Caflisch, A.
Binding Motifs in the CBP Bromodomain: An Analysis of 20 Crystal Structures of Complexes with Small Molecules.
ACS Med Chem Lett, 9:929-934, 2018
Cited by
PubMed Abstract: We analyze 20 crystal structures of complexes between the CBP bromodomain and small-molecule ligands that belong to eight different chemotypes identified by docking. The binding motif of the moiety that mimics the natural ligand (acetylated side chain of lysine) at the bottom of the binding pocket is conserved. In stark contrast, the rest of the ligands form different interactions with different side chains and backbone polar groups on the outer rim of the binding pocket. Hydrogen bonds are direct or water-bridged. van der Waals contacts are optimized by rotations of hydrophobic side chains and a slight inward displacement of the ZA loop. Rare types of interactions are observed for some of the ligands.
PubMed: 30258543
DOI: 10.1021/acsmedchemlett.8b00286
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

238582

數據於2025-07-09公開中

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