7QOB
Human Carbonic Anhydrase I in complex with benzoselenoate
This is a non-PDB format compatible entry.
Summary for 7QOB
| Entry DOI | 10.2210/pdb7qob/pdb |
| Descriptor | Carbonic anhydrase 1, ZINC ION, benzoselenoate, ... (4 entities in total) |
| Functional Keywords | carbonic anhydrase i, inhibitor, metalloenzyme, benzoselenoate, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 58313.35 |
| Authors | Angeli, A.,Ferraroni, M. (deposition date: 2021-12-23, release date: 2023-01-18, Last modification date: 2024-01-31) |
| Primary citation | Tanini, D.,Capperucci, A.,Locuoco, M.,Ferraroni, M.,Costantino, G.,Angeli, A.,Supuran, C.T. Benzoselenoates: A novel class of carbonic anhydrase inhibitors. Bioorg.Chem., 122:105751-105751, 2022 Cited by PubMed Abstract: A series of benzoselenoates has been prepared and their inhibitory properties against the most relevant human Carbonic Anhydrases (CAs) isoforms, among which hCA I, II, IV, VII, IX, and XII were investigated. These inhibitors were designed considering the carboxylates and mono-/dithiocarbamates as lead and led to the observation that the COSe is a new zinc-binding group (ZBG) for metalloenzymes possessing zinc ions at their active site. The substitution pattern on aromatic ring of the benzoselenoates is the crucial structural element influencing selectivity towards various isoforms. We elucidated the binding mode of benzoselenoates to hCA I and hCA II by using X-ray crystallography. The negatively charged selenium atom from the new ZBG was observed coordinated to the zinc ion from the CA active site at a distance of 2.30-2.40 Å from it. Overall, these data might be useful for the development of new inhibitors with higher selectivity and efficacy for various hCAs. PubMed: 35344894DOI: 10.1016/j.bioorg.2022.105751 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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