5F36

Crystal structure of the bromodomain of human ATAD2 in complex with Compound A12

Summary for 5F36

• Entry DOI: 10.2210/pdb5f36/pdb
• Descriptor: ATPase family AAA domain-containing protein 2, [(2~{R})-1-[(4-ethanoyl-1,3-thiazol-2-yl)amino]-1-oxidanylidene-propan-2-yl]azanium, SULFATE ION, ... (5 entities in total)
• Functional Keywords: hydrolase inhibitor complex, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 15799.29

Authors

Dong, J.,Caflisch, A. (deposition date: 2015-12-02, release date: 2016-12-14, Last modification date: 2024-01-10)

Primary citation

Dolbois, A.,Batiste, L.,Wiedmer, L.,Dong, J.,Brutsch, M.,Huang, D.,Deerain, N.M.,Spiliotopoulos, D.,Cheng-Sanchez, I.,Laul, E.,Nevado, C.,Sledz, P.,Caflisch, A.
Hitting a Moving Target: Simulation and Crystallography Study of ATAD2 Bromodomain Blockers.
Acs Med.Chem.Lett., 11:1573-1580, 2020

PubMed Abstract: Small molecule ligand binding to the ATAD2 bromodomain is investigated here through the synergistic combination of molecular dynamics and protein crystallography. A previously unexplored conformation of the binding pocket upon rearrangement of the gatekeeper residue Ile1074 has been found. Further, our investigations reveal how minor structural differences in the ligands result in binding with different plasticity of the ZA loop for this difficult-to-drug bromodomain.

PubMed: 32832026
DOI: 10.1021/acsmedchemlett.0c00080

Experimental method

X-RAY DIFFRACTION (1.5 Å)