3FFP
X ray structure of the complex between carbonic anhydrase II and LC inhibitors
Summary for 3FFP
| Entry DOI | 10.2210/pdb3ffp/pdb |
| Descriptor | Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (6 entities in total) |
| Functional Keywords | carbonic anhydrase, inhibitors, acetylation, cytoplasm, disease mutation, lyase, metal-binding, polymorphism, zinc |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29957.51 |
| Authors | Temperini, C.,Crocetti, L.,Scozzafava, A.,Supuran, C.T. (deposition date: 2008-12-04, release date: 2009-08-18, Last modification date: 2023-11-01) |
| Primary citation | Crocetti, L.,Maresca, A.,Temperini, C.,Hall, R.A.,Scozzafava, A.,Muhlschlegel, F.A.,Supuran, C.T. A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases Bioorg.Med.Chem.Lett., 19:1371-1375, 2009 Cited by PubMed Abstract: A sulfonamide derivative of the antihelmintic drug thiabendazole was prepared and investigated for inhibition of the zinc enzyme carbonic anhydrase CA (EC 4.2.1.1). Mammalian isoforms CA I-XIV and the nematode enzyme of Caenorhabditis elegans CAH-4b were included in this study. Thiabendazole-5-sulfonamide was a very effective inhibitor of CAH-4b and CA IX (K(I)s of 6.4-9.5nm) and also inhibited effectively isozymes CA I, II, IV-VII, and XII, with K(I)s in the range of 17.8-73.2nM. The high resolution X-ray crystal structure of its adduct with isozyme II evidenced the structural elements responsible for this potent inhibitory activity. PubMed: 19186056DOI: 10.1016/j.bmcl.2009.01.038 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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