4Q6E

Crystal structure of human carbonic anhydrase isozyme II with 4-{[3-(3,5-Dimethyl-1H-pyrazol-1-yl)-3-oxopropyl]amino}benzene-1-sulfonamide

Summary for 4Q6E

• Entry DOI: 10.2210/pdb4q6e/pdb
• Related: 4Q6D
• Descriptor: Carbonic anhydrase 2, ZINC ION, BICINE, ... (6 entities in total)
• Functional Keywords: drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, lyase/lyase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P00918
• Total number of polymer chains: 1
• Total formula weight: 29996.29

Authors

Smirnov, A.,Manakova, E.,Grazulis, S. (deposition date: 2014-04-22, release date: 2014-11-26, Last modification date: 2023-09-20)

Primary citation

Rutkauskas, K.,Zubriene, A.,Tumosiene, I.,Kantminiene, K.,Kazemekaite, M.,Smirnov, A.,Kazokaite, J.,Morkunaite, V.,Capkauskaite, E.,Manakova, E.,Grazulis, S.,Beresnevicius, Z.J.,Matulis, D.
4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.
Molecules, 19:17356-17380, 2014

PubMed Abstract: A series of N-aryl-β-alanine derivatives and diazobenzenesulfonamides containing aliphatic rings were designed, synthesized, and their binding to carbonic anhydrases (CA) I, II, VI, VII, XII, and XIII was studied by the fluorescent thermal shift assay and isothermal titration calorimetry. The results showed that 4-substituted diazobenzenesulfonamides were more potent CA binders than N-aryl-β-alanine derivatives. Most of the N-aryl-β-alanine derivatives showed better affinity for CA II while diazobenzenesulfonamides possessed nanomolar affinities towards CA I isozyme. X-ray crystallographic structures showed the modes of binding of both compound groups.

PubMed: 25353386
DOI: 10.3390/molecules191117356

Experimental method

X-RAY DIFFRACTION (1.12 Å)