2FW4
Carbonic anhydrase activators. The first X-ray crystallographic study of an activator of isoform I, structure with L-histidine.
Summary for 2FW4
| Entry DOI | 10.2210/pdb2fw4/pdb |
| Descriptor | Carbonic anhydrase 1, ZINC ION, HISTIDINE, ... (4 entities in total) |
| Functional Keywords | carbonic anhydrase i, activators, lyase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P00915 |
| Total number of polymer chains | 2 |
| Total formula weight | 57993.12 |
| Authors | Temperini, C.,Scozzafava, A.,Supuran, C.T. (deposition date: 2006-02-01, release date: 2006-08-08, Last modification date: 2024-02-14) |
| Primary citation | Temperini, C.,Scozzafava, A.,Supuran, C.T. Carbonic anhydrase activators: The first X-ray crystallographic study of an adduct of isoform I. Bioorg.Med.Chem.Lett., 16:5152-5156, 2006 Cited by PubMed Abstract: The X-ray crystallographic structure for the adduct of an activator with human carbonic anhydrase isozyme I (hCA I) is reported. L-Histidine binds deep within the enzyme active site, participating in a network of hydrogen bonds involving its carboxylate moiety and the zinc-bound water molecule, as well as the imidazole of His200, being in van der Waals contacts with Thr199, His200, His64, and His67. This binding is very different from that to the other major cytosolic isozyme hCA II. PubMed: 16870440DOI: 10.1016/j.bmcl.2006.07.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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