8BZZ

Crystal structure of carbonic anhydrase 2 4-(dimethylamino)-N-nitrobenzenesulfonamide

This is a non-PDB format compatible entry.

Summary for 8BZZ

• Entry DOI: 10.2210/pdb8bzz/pdb
• Descriptor: Carbonic anhydrase 2, GLYCEROL, ZINC ION, ... (5 entities in total)
• Functional Keywords: carbonic anhydrase 2, n-nitrobenzenesulfonamide, metalloenzyme, inhibitor, lyase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 29937.08

Authors

Angeli, A.,Ferraroni, M. (deposition date: 2022-12-15, release date: 2023-12-27, Last modification date: 2024-07-10)

Primary citation

Angeli, A.,Ferraroni, M.,Bonardi, A.,Supuran, C.T.,Nocentini, A.
Diversely N -substituted benzenesulfonamides dissimilarly bind to human carbonic anhydrases: crystallographic investigations of N -nitrosulfonamides.
J Enzyme Inhib Med Chem, 38:2178430-2178430, 2023

PubMed Abstract: Carbonic anhydrases (CAs) are a zinc metalloenzymes that catalyse the reversible hydration of carbon dioxide to bicarbonate and proton, pivotal for a wide range of biological processes. CAs are involved in numerous pathologies and thus represent valuable drug targets in the treatments of several diseases such as glaucoma, obesity, tumour, neuropathic pain, cerebral ischaemia, or as antiinfectives. In the last two decades, several efforts have been made to achieve selective CA inhibitors (CAIs) employing different drug design approaches. However, -substitutions on primary sulphonamide groups still remain poorly investigated. Here, we reported for the first time the co-crystallisation of a -nitro sulphonamide derivative with human (h) CA II pointing out the binding site and mode of inhibition of this class of CAIs. The thorough comprehension of the ligand/target interaction might be valuable for a further CAI optimisation for achieving new potent and selective derivatives.

PubMed: 36798036
DOI: 10.1080/14756366.2023.2178430

Experimental method

X-RAY DIFFRACTION (1.07 Å)