2VCG
Crystal structure of a HDAC-like protein HDAH from Bordetella sp. with the bound inhibitor ST-17
Summary for 2VCG
| Entry DOI | 10.2210/pdb2vcg/pdb |
| Related | 1ZZ0 1ZZ1 1ZZ3 |
| Descriptor | HISTONE DEACETYLASE-LIKE AMIDOHYDROLASE, ZINC ION, POTASSIUM ION, ... (7 entities in total) |
| Functional Keywords | hdah, inhibitor, hdac-like amidohydrolase, hydrolase, histone deacetylase-like amidohydrolase |
| Biological source | ALCALIGENES SP. |
| Total number of polymer chains | 4 |
| Total formula weight | 163590.61 |
| Authors | Dickmanns, A.,Strasser, A.,Ficner, R. (deposition date: 2007-09-24, release date: 2008-01-08, Last modification date: 2023-12-13) |
| Primary citation | Schaefer, S.,Saunders, L.,Eliseeva, E.,Velena, A.,Jung, M.,Schwienhorst, A.,Strasser, A.,Dickmanns, A.,Ficner, R.,Schlimme, S.,Sippl, W.,Verdin, E.,Jung, M. Phenylalanine-Containing Hydroxamic Acids as Selective Inhibitors of Class Iib Histone Deacetylases (Hdacs). Bioorg.Med.Chem., 16:2011-, 2008 Cited by PubMed Abstract: We synthesized biarylalanine-containing hydroxamic acids and tested them on immunoprecipitated HDAC1 and HDAC6 and show a subtype selectivity for HDAC6 that was confirmed in cells by Western blot (tubulin vs histones). We obtained an X-ray structure with a HDAC6-selective inhibitor with the bacterial deacetylase HDAH. Docking studies were carried out using HDAC1 and HDAC6 protein models. Antiproliferative activity was shown on cancer cells for selected compounds. PubMed: 18054239DOI: 10.1016/J.BMC.2007.10.092 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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