4XE1
Human carbonic anhydrase II in complex with 6-SULFAMOYL-SACCHARIN
Summary for 4XE1
| Entry DOI | 10.2210/pdb4xe1/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | cytoplasm, lyase, inhibitor |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 30327.88 |
| Authors | Alterio, V.,De Simone, G. (deposition date: 2014-12-21, release date: 2015-03-18, Last modification date: 2024-01-10) |
| Primary citation | Alterio, V.,Tanc, M.,Ivanova, J.,Zalubovskis, R.,Vozny, I.,Monti, S.M.,Di Fiore, A.,De Simone, G.,Supuran, C.T. X-ray crystallographic and kinetic investigations of 6-sulfamoyl-saccharin as a carbonic anhydrase inhibitor. Org.Biomol.Chem., 13:4064-4069, 2015 Cited by PubMed Abstract: 6-Sulfamoyl-saccharin was investigated as an inhibitor of 11 α-carbonic anhydrase (CA, EC 4.2.1.1) isoforms of human (h) origin, hCA I-XIV, and X-ray crystallographic data were obtained for its adduct with hCA II, the physiologically dominant isoform. This compound possesses two potential zinc-binding groups, the primary sulfamoyl one and the secondary, acylatedsulfonamide. Saccharin itself binds to the Zn(II) ion from the CA active site coordinating with this last group, in deprotonated (SO2N(-)CO) form. Here we explain why 6-sulfamoyl-saccharin, unlike saccharin, binds to the metal ion from the hCA II active site by its primary sulfonamide moiety and not the secondary one as saccharin itself. Our study is useful for shedding new light to the structure-based drug design of isoform-selective CA inhibitors of the sulfonamide type. PubMed: 25733161DOI: 10.1039/c4ob02648a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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