3M96
Crystal structure of human carbonic anhydrase isozyme II with 5-{[(5-bromo-1H-benzimidazol-2-yl)sulfanyl]acetyl}-2-chlorobenzenesulfonamide
Summary for 3M96
| Entry DOI | 10.2210/pdb3m96/pdb |
| Related | 3M98 |
| Descriptor | Carbonic anhydrase 2, ZINC ION, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | drug design, carbonic anhydrase, benzenesulfonamide, lyase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29971.49 |
| Authors | Grazulis, S.,Manakova, E.,Golovenko, D. (deposition date: 2010-03-20, release date: 2011-02-02, Last modification date: 2023-09-06) |
| Primary citation | Baranauskiene, L.,Golovenko, D.,Manakova, E.,Grazulis, S.,Tumkevicius, S.,Matulis, D. Indapamide-like benzenesulfonamides as inhibitors of carbonic anhydrases I, II, VII, and XIII. Bioorg.Med.Chem., 18:7357-7364, 2010 Cited by PubMed Abstract: A series of novel 2-chloro-5-[(1-benzimidazolyl- and 2-benzimidazolylsulfanyl)acetyl]benzene-sulfonamides were designed and synthesized. Their binding to recombinant human carbonic anhydrase (hCA) isozymes I, II, VII, and XIII was determined by isothermal titration calorimetry and thermal shift assay. The designed S-alkylated benzimidazole derivatives exhibited stronger binding than the indapamide-like N-alkylated benzimidazoles, with the K(d) reaching about 50-100 nM with drug-targeted hCAs VII and XIII. The cocrystal structures of selected compounds with hCA II were determined by X-ray crystallography, and structural features of the binding event were revealed. PubMed: 20926301DOI: 10.1016/j.bmc.2010.09.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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