2GEH
N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
Summary for 2GEH
Entry DOI | 10.2210/pdb2geh/pdb |
Descriptor | Carbonic anhydrase 2, ZINC ION, MERCURY (II) ION, ... (5 entities in total) |
Functional Keywords | carbonic anhydrase, inhibitors, lyase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm : P00918 |
Total number of polymer chains | 1 |
Total formula weight | 29831.71 |
Authors | Temperini, C.,Innocenti, A.,Scozzafava, A.,Supuran, C.T. (deposition date: 2006-03-20, release date: 2006-06-20, Last modification date: 2024-02-14) |
Primary citation | Temperini, C.,Innocenti, A.,Scozzafava, A.,Supuran, C.T. N-Hydroxyurea-A versatile zinc binding function in the design of metalloenzyme inhibitors. Bioorg.Med.Chem.Lett., 16:4316-4320, 2006 Cited by PubMed Abstract: N-Hydroxyurea binds both to carbonic anhydrase (CA) and to matrix metalloproteinases (MMPs). X-ray crystallography showed N-hydroxyurea to bind in a bidentate mode by means of the oxygen and nitrogen atoms of the NHOH moiety to the Zn(II) ion of CA, participating in a network of hydrogen bonds with a water molecule and Thr199. A derivatized N-hydroxyurea showed low-micromolar affinity for several CAs. This simple zinc binding function may be exploited for obtaining potent metalloenzyme inhibitors, due to its versatility of binding to the metal ion present in the active site of such enzymes. PubMed: 16759856DOI: 10.1016/j.bmcl.2006.05.068 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
