9GFX
Huma Carbonic anhydrase II in complex with trans-2-phenylvinylboronic acid
This is a non-PDB format compatible entry.
Summary for 9GFX
| Entry DOI | 10.2210/pdb9gfx/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, tris(oxidanyl)-[(~{E})-2-phenylethenyl]boron, ... (5 entities in total) |
| Functional Keywords | carbonic anhydrase ii, protein-inhibitor complex, inhibitor, boronic acid, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29611.54 |
| Authors | Alterio, V.,De Simone, G.,Esposito, D. (deposition date: 2024-08-12, release date: 2024-11-06, Last modification date: 2024-11-13) |
| Primary citation | Esposito, D.,Monti, S.M.,Supuran, C.T.,Winum, J.Y.,De Simone, G.,Alterio, V. Exploring the binding mode of phenyl and vinyl boronic acids to human carbonic anhydrases. Int.J.Biol.Macromol., 282:136873-136873, 2024 Cited by PubMed Abstract: Boronic acids are an interesting but still poorly studied class of carbonic anhydrase inhibitors. Previous investigations proved that derivatives incorporating aromatic, arylalkyl, and arylalkenyl moieties are low micromolar to millimolar inhibitors for several α- and β-CAs involved in pathologic states. Here we report a high-resolution X-ray study on two classes of boronic acids (phenyl and vinyl) in complex with hCA II. Our results unambiguously clarify the binding mode of these molecules to the human carbonic anhydrase active site, which occurs through their tetrahedral anionic form, regardless of the nature of the organic scaffold. Data here presented contribute to the understanding of the inhibition mechanism of boronic acids that can be fruitfully used for the rational design of novel and effective isozyme-specific carbonic anhydrase inhibitors. PubMed: 39454912DOI: 10.1016/j.ijbiomac.2024.136873 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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