3D0N
Crystal structure of human carbonic anhydrase XIII
Summary for 3D0N
Entry DOI | 10.2210/pdb3d0n/pdb |
Related | 1CA2 |
Descriptor | Carbonic anhydrase 13, ZINC ION, ACETATE ION, ... (5 entities in total) |
Functional Keywords | carbonic anhydrase, lyase, metal-binding, metal binding protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 59593.50 |
Authors | Di Fiore, A.,De Simone, G. (deposition date: 2008-05-02, release date: 2008-07-29, Last modification date: 2023-08-30) |
Primary citation | Di Fiore, A.,Monti, S.M.,Hilvo, M.,Parkkila, S.,Romano, V.,Scaloni, A.,Pedone, C.,Scozzafava, A.,Supuran, C.T.,De Simone, G. Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide. Proteins, 74:164-175, 2008 Cited by PubMed Abstract: The cytosolic isoform XIII is a recently discovered member of the human carbonic anhydrase (hCA, EC 4.2.1.1) family. It is selectively expressed among other tissues in the reproductive organs, where it may control pH and ion balance regulation, ensuring thus proper fertilization conditions. The authors report here the X-ray crystallographic structure of this isozyme in the unbound state and in complex with a classical sulfonamide inhibitor, namely acetazolamide. A detailed comparison of the obtained structural data with those already reported for other CA isozymes provides novel insights into the catalytic properties of the members of this protein family. On the basis of the inhibitory properties of acetazolamide against various cytosolic/transmembrane isoforms and the structural differences detected within the active site of the various CA isoforms, further prospects for the design of isozyme-specific CA inhibitors are here proposed. PubMed: 18618712DOI: 10.1002/prot.22144 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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