3max | pdb_00003max

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

spinqualitylabelsall models 3max, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3max is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, LLX, NA, NHE, ZN Gene: HDAC2 (Homo sapiens) Activity: Histone deacetylase, with EC number 3.5.1.98 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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). Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides.,Bressi JC, Jennings AJ, Skene R, Wu Y, Melkus R, De Jong R, O'Connell S, Grimshaw CE, Navre M, Gangloff AR Bioorg Med Chem Lett. 2010 May 15;20(10):3142-5. Epub 2010 Mar 30. PMID:20392638 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Histone deacetylase

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