3MHI

Crystal structure of human carbonic anhydrase isozyme II with 4-{[(5-nitro-6-oxo-1,6-dihydro-4-pyrimidinyl)amino]methyl}benzenesulfonamide

Summary for 3MHI

• Entry DOI: 10.2210/pdb3mhi/pdb
• Related: 3M2N 3M3X 3M40 3M5E 3MHL 3MHM 3MHO
• Descriptor: Carbonic anhydrase 2, ZINC ION, 4-{[(5-nitro-6-oxo-1,6-dihydropyrimidin-4-yl)amino]methyl}benzenesulfonamide, ... (5 entities in total)
• Functional Keywords: drug design, carbonic anhydrase, sulfonamide, 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: 30161.34

Authors

Grazulis, S.,Manakova, E.,Golovenko, D. (deposition date: 2010-04-08, release date: 2010-10-20, Last modification date: 2023-11-01)

Primary citation

Sudzius, J.,Baranauskiene, L.,Golovenko, D.,Matuliene, J.,Michailoviene, V.,Torresan, J.,Jachno, J.,Sukackaite, R.,Manakova, E.,Grazulis, S.,Tumkevicius, S.,Matulis, D.
4-[N-(Substituted 4-pyrimidinyl)amino]benzenesulfonamides as inhibitors of carbonic anhydrase isozymes I, II, VII, and XIII
Bioorg.Med.Chem., 18:7413-7421, 2010

PubMed Abstract: A series of 4-[N-(substituted 4-pyrimidinyl)amino]benzenesulfonamides were designed and synthesised. Their binding potencies as inhibitors of selected recombinant human carbonic anhydrase (hCA) isozymes I, II, VII, and XIII were measured using isothermal titration calorimetry and the thermal shift assay. To determine the structural features of inhibitor binding, the crystal structures of several compounds in complex with hCA II were determined. Several compounds exhibited selectivity towards isozymes I, II, and XIII, and some were potent inhibitors of hCA VII.

PubMed: 20889345
DOI: 10.1016/j.bmc.2010.09.011

Experimental method

X-RAY DIFFRACTION (1.7 Å)