3K7K
Crystal structure of the complex between Carbonic Anhydrase II and anions
Summary for 3K7K
| Entry DOI | 10.2210/pdb3k7k/pdb |
| Related | 1BV3 |
| Descriptor | Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (5 entities in total) |
| Functional Keywords | inorganic anion, trithiocarbonate, x ray, carbonic anhydrase ii, lyase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29665.28 |
| Authors | Temperini, C. (deposition date: 2009-10-13, release date: 2010-01-26, Last modification date: 2023-11-01) |
| Primary citation | Temperini, C.,Scozzafava, A.,Supuran, C.T. Carbonic anhydrase inhibitors. X-ray crystal studies of the carbonic anhydrase II-trithiocarbonate adduct-An inhibitor mimicking the sulfonamide and urea binding to the enzyme Bioorg.Med.Chem.Lett., 20:474-478, 2010 Cited by PubMed Abstract: Trithiocarbonate (CS32-) inhibits with low micromolar affinities several mammalian carbonic anhydrases, CAs, EC 4.2.1.1 [Innocenti et al., Bioorg. Med. Chem. Lett. 2009, 19, 1855]. Here we report the X-ray crystal structure of the hCA II-trithiocarbonate adduct. Trithiocarbonate is monodentately bound to the Zn(II) ion and makes several hydrogen bonds with Thr199 and two water molecules from the enzyme active site. Its binding is different from that of ureate, another small inhibitor isosteric with trithiocarbonate but somehow mimicks the binding of the SO(2)NH moiety present in the sulfonamide inhibitors and is similar to that of bicarbonate. Compounds incorporating this new zinc-binding group, CS2-, may thus lead to new classes of potent inhibitors. PubMed: 20005709DOI: 10.1016/j.bmcl.2009.11.124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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