7QGZ
Human carbonic anhydrase II in complex with Methyl 3-((4-methylthiazol-2-yl)(4-sulfamoylphenyl)amino)propanoate
Summary for 7QGZ
| Entry DOI | 10.2210/pdb7qgz/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, methyl 3-[(4-methyl-1,3-thiazol-2-yl)-(4-sulfamoylphenyl)amino]propanoate, ... (4 entities in total) |
| Functional Keywords | drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29709.90 |
| Authors | Paketuryte-Latve, V.,Smirnov, A.,Manakova, E.,Grazulis, S. (deposition date: 2021-12-10, release date: 2022-05-04, Last modification date: 2024-01-31) |
| Primary citation | Balandis, B.,Simkunas, T.,Paketuryte-Latve, V.,Michailoviene, V.,Mickeviciute, A.,Manakova, E.,Grazulis, S.,Belyakov, S.,Kairys, V.,Mickevicius, V.,Zubriene, A.,Matulis, D. Beta and Gamma Amino Acid-Substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases. Pharmaceuticals, 15:-, 2022 Cited by PubMed Abstract: A series of novel benzenesulfonamide derivatives were synthesized bearing - β,γ-amino acid or - β-amino acid and thiazole moieties and their binding to the human carbonic anhydrase (CA) isozymes determined. These enzymes are involved in various illnesses, such as glaucoma, altitude sickness, epilepsy, obesity, and even cancer. There are numerous compounds that are inhibitors of CA and used as pharmaceuticals. However, most of them bind to most CA isozymes with little selectivity. The design of high affinity and selectivity towards one CA isozyme remains a significant challenge. The beta and gamma amino acid-substituted compound affinities were determined by the fluorescent thermal shift assay and isothermal titration calorimetry for all 12 catalytically active human carbonic anhydrase isozymes, showing the full affinity and selectivity profile. The structures of several compounds were determined by X-ray crystallography, and the binding mode in the active site of CA enzyme was shown. PubMed: 35455474DOI: 10.3390/ph15040477 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.13 Å) |
Structure validation
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