3MAX

Crystal Structure of Human HDAC2 complexed with an N-(2-aminophenyl)benzamide

Summary for 3MAX

• Entry DOI: 10.2210/pdb3max/pdb
• Descriptor: Histone deacetylase 2, ZINC ION, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: class 2, hdac, foot pocket, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q92769
• Total number of polymer chains: 3
• Total formula weight: 127895.75

Authors

Skene, R.J.,Jennings, A.J. (deposition date: 2010-03-24, release date: 2010-04-28, Last modification date: 2024-02-21)

Primary citation

Bressi, J.C.,Jennings, A.J.,Skene, R.,Wu, Y.,Melkus, R.,De Jong, R.,O'Connell, S.,Grimshaw, C.E.,Navre, M.,Gangloff, A.R.
Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides.
Bioorg.Med.Chem.Lett., 20:3142-3145, 2010

PubMed Abstract: A series of N-(2-amino-5-substituted phenyl)benzamides (3-21) were designed, synthesized and evaluated for their inhibition of HDAC2 and their cytotoxicity in HCT116 cancer cells. Multiple compounds from this series demonstrated time-dependent binding kinetics that is rationalized using a co-complex crystal structure of HDAC2 and N-(4-aminobiphenyl-3-yl)benzamide (6).

PubMed: 20392638
DOI: 10.1016/j.bmcl.2010.03.091

Experimental method

X-RAY DIFFRACTION (2.05 Å)