2Q1Q
Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-Ray crystallographic studies
Summary for 2Q1Q
| Entry DOI | 10.2210/pdb2q1q/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (5 entities in total) |
| Functional Keywords | antiepileptic, carbonic anhydrase, inhibitors, lyase |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29845.42 |
| Authors | Temperini, C.,Innocenti, A.,Mastrolorenzo, A.,Scozzafava, A.,Supuran, C.T. (deposition date: 2007-05-25, release date: 2007-09-11, Last modification date: 2024-02-21) |
| Primary citation | Temperini, C.,Innocenti, A.,Mastrolorenzo, A.,Scozzafava, A.,Supuran, C.T. Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: Kinetic and X-ray crystallographic studies. Bioorg.Med.Chem.Lett., 17:4866-4872, 2007 Cited by PubMed Abstract: Sulthiame, a clinically used antiepileptic, was investigated for its interaction with 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms. The drug is a potent inhibitor of CA II, VII, IX, and XII (K(I)s of 6-56 nM), and a medium potency inhibitor against CA IV, VA, VB, and VI (K(I)s of 81-134 nM). The high resolution crystal structure of the hCA II-sulthiame adduct revealed a large number of favorable interactions between the drug and the enzyme which explain its strong low nanomolar affinity for this isoform and may also be exploited for the design of effective inhibitors incorporating sultam moieties. PubMed: 17588751DOI: 10.1016/j.bmcl.2007.06.044 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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