8OGF
Human Carbonic Anhydrase II in complex with 4-(((1-(3-((3aR,7R,7aS)-7-hydroxy-2,2-dimethyltetrahydro-[1,3]dioxolo[4,5-c]pyridin-5(4H)-yl)propyl)-1H-1,2,3-triazol-4-yl)methyl)amino)benzenesulfonamide
This is a non-PDB format compatible entry.
Summary for 8OGF
| Entry DOI | 10.2210/pdb8ogf/pdb |
| Descriptor | Carbonic anhydrase 2, GLYCEROL, ZINC ION, ... (5 entities in total) |
| Functional Keywords | carbonic anhydrase, sulfonamide, inhibitor, metalloenzyme, iminosugar, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 30383.71 |
| Authors | Angeli, A.,Ferraroni, M. (deposition date: 2023-03-20, release date: 2024-03-27, Last modification date: 2025-10-08) |
| Primary citation | Davighi, M.G.,Matassini, C.,Goti, A.,Ferraroni, M.,Angeli, A.,Supuran, C.T.,Cardona, F. Mono- and three-tailed sugar and iminosugar decorated benzenesulfonamide carbonic anhydrase inhibitors. Org.Biomol.Chem., 21:4491-4503, 2023 Cited by PubMed Abstract: A collection of novel mono- and three-tailed derivatives based on a sugar (glucose) or an iminosugar (trihydroxy piperidine) featuring a terminal benzenesulfonamide were synthesized to investigate the so-called "sugar" and "azasugar" approach with the aim of exploring the activity and selectivity towards the inhibition of human carbonic anhydrases (hCAs). The synthetic approach relies on a general copper(I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction followed by an amine-isothiocyanate coupling. Biological assays were used to collect subtle information on the role of these single or multiple hydrophilic chains. Among the sugar-based inhibitors, the single-tailed compound 10 was identified as a better inhibitor than the reference compound (AAZ) towards three different hCAs, while, among the three sugar tailed derivatives, potent and selective inhibition was found for compounds 25 and 26. A promising and selective inhibitory activity was discovered for the iminosugar single-tailed compound 31 towards hCA VII (Ki = 9.7 nM). PubMed: 37198937DOI: 10.1039/d3ob00529a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.321 Å) |
Structure validation
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