6GWU
Carbonic anhydrase CaNce103p from Candida albicans
Summary for 6GWU
| Entry DOI | 10.2210/pdb6gwu/pdb |
| Descriptor | Carbonic anhydrase, ZINC ION, BETA-MERCAPTOETHANOL, ... (6 entities in total) |
| Functional Keywords | carbonic anhydrase, candida albicans, cance103p, substrate tunnel, lyase |
| Biological source | Candida albicans (Yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 93197.89 |
| Authors | Brynda, J.,Dostal, J.,Heidingsfeld, O.,Machacek, S.,Blaha, J.,Pichova, I. (deposition date: 2018-06-26, release date: 2018-11-07, Last modification date: 2024-01-17) |
| Primary citation | Dostal, J.,Brynda, J.,Blaha, J.,Machacek, S.,Heidingsfeld, O.,Pichova, I. Crystal structure of carbonic anhydrase CaNce103p from the pathogenic yeast Candida albicans. BMC Struct. Biol., 18:14-14, 2018 Cited by PubMed Abstract: The pathogenic yeast Candida albicans can proliferate in environments with different carbon dioxide concentrations thanks to the carbonic anhydrase CaNce103p, which accelerates spontaneous conversion of carbon dioxide to bicarbonate and vice versa. Without functional CaNce103p, C. albicans cannot survive in atmospheric air. CaNce103p falls into the β-carbonic anhydrase class, along with its ortholog ScNce103p from Saccharomyces cerevisiae. The crystal structure of CaNce103p is of interest because this enzyme is a potential target for surface disinfectants. PubMed: 30367660DOI: 10.1186/s12900-018-0093-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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