1CRA
THE COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND THE AROMATIC INHIBITOR 1,2,4-TRIAZOLE
Summary for 1CRA
| Entry DOI | 10.2210/pdb1cra/pdb |
| Descriptor | CARBONIC ANHYDRASE II, ZINC ION, MERCURY (II) ION, ... (5 entities in total) |
| Functional Keywords | lyase(oxo-acid) |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P00918 |
| Total number of polymer chains | 1 |
| Total formula weight | 29518.97 |
| Authors | Mangani, S.,Liljas, A. (deposition date: 1992-10-21, release date: 1994-01-31, Last modification date: 2024-10-30) |
| Primary citation | Mangani, S.,Liljas, A. Crystal structure of the complex between human carbonic anhydrase II and the aromatic inhibitor 1,2,4-triazole. J.Mol.Biol., 232:9-14, 1993 Cited by PubMed Abstract: The X-ray crystal structure of the complex between human carbonic anhydrase II and the inhibitor 1,2,4-triazole has been refined at 1.9 A resolution to a final R-factor of 0.153. Triazole is an analogue of the competitive inhibitor imidazole, but the crystal structure shows a different type of binding to the enzyme. 1,2,4-Triazole is directly bound to the zinc(II) ion through the nitrogen in position 4, replacing the native water/hydroxyl (Wat263) in a distorted four-co-ordinated complex. The interaction of the inhibitor with the active site is completed by two hydrogen bonds to O gamma of Thr200 and to the amide nitrogen atom of Thr199 through the two adjacent N-1 and N-2 atoms. The binding site of triazole overlaps the proposed binding sites for the substrates, explaining the observed competitive behaviour of the inhibitor towards CO2/HCO3- under equilibrium conditions. PubMed: 8331673DOI: 10.1006/jmbi.1993.1365 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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