5H8X
Crystal structure of the complex MMP-8/BF471 (catechol inhibitor)
Summary for 5H8X
| Entry DOI | 10.2210/pdb5h8x/pdb |
| Descriptor | Neutrophil collagenase, CALCIUM ION, ZINC ION, ... (7 entities in total) |
| Functional Keywords | catechol function, mmps, inhibitor, metalloprotese, zinc binding function, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasmic granule: P22894 |
| Total number of polymer chains | 1 |
| Total formula weight | 19200.72 |
| Authors | Pochetti, G.,Montanari, R.,Capelli, D.,Tortorella, P. (deposition date: 2015-12-24, release date: 2016-11-02, Last modification date: 2024-01-10) |
| Primary citation | Tauro, M.,Laghezza, A.,Loiodice, F.,Piemontese, L.,Caradonna, A.,Capelli, D.,Montanari, R.,Pochetti, G.,Di Pizio, A.,Agamennone, M.,Campestre, C.,Tortorella, P. Catechol-based matrix metalloproteinase inhibitors with additional antioxidative activity. J Enzyme Inhib Med Chem, 31:25-37, 2016 Cited by PubMed Abstract: New catechol-containing chemical entities have been investigated as matrix metalloproteinase inhibitors as well as antioxidant molecules. The combination of the two properties could represent a useful feature due to the potential application in all the pathological processes characterized by increased proteolytic activity and radical oxygen species (ROS) production, such as inflammation and photoaging. A series of catechol-based molecules were synthesized and tested for both proteolytic and oxidative inhibitory activity, and the detailed binding mode was assessed by crystal structure determination of the complex between a catechol derivative and the matrix metalloproteinase-8. Surprisingly, X-ray structure reveals that the catechol oxygens do not coordinates the zinc atom. PubMed: 27556138DOI: 10.1080/14756366.2016.1217853 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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