3H0J

Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with compound 2

Summary for 3H0J

• Entry DOI: 10.2210/pdb3h0j/pdb
• Related: 3H0Q 3H0S
• Descriptor: Acetyl-CoA carboxylase, 6-{[1-(anthracen-9-ylcarbonyl)piperidin-4-yl]methyl}-2-methylquinoline (2 entities in total)
• Functional Keywords: transferase, acetyl-coa carboxylase, carboxyltransferase, inhibitor, acc, ct, atp-binding, biotin, cytoplasm, fatty acid biosynthesis, ligase, lipid synthesis, metal-binding, multifunctional enzyme, nucleotide-binding
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: Q00955
• Total number of polymer chains: 3
• Total formula weight: 263047.63

Authors

Zhang, H.,Tong, L. (deposition date: 2009-04-09, release date: 2010-04-07, Last modification date: 2024-02-21)

• Primary citation: Corbett, J.W.,Freeman-Cook, K.D.,Elliott, R.,Vajdos, F.,Rajamohan, F.,Kohls, D.,Marr, E.,Zhang, H.,Tong, L.,Tu, M.,Murdande, S.,Doran, S.D.,Houser, J.A.,Song, W.,Jones, C.J.,Coffey, S.B.,Buzon, L.,Minich, M.L.,Dirico, K.J.,Tapley, S.,McPherson, R.K.,Sugarman, E.,Harwood, H.J.,Esler, W.; Discovery of small molecule isozyme non-specific inhibitors of mammalian acetyl-CoA carboxylase 1 and 2.; Bioorg.Med.Chem.Lett., 20:2383-2388, 2010; PubMed: 20219367; DOI: 10.1016/j.bmcl.2009.04.091

Experimental method

X-RAY DIFFRACTION (2.8 Å)