3EHX
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (R)-2-(biphenyl-4-ylsulfonamido)-4-methylpentanoic acid
Summary for 3EHX
| Entry DOI | 10.2210/pdb3ehx/pdb |
| Related | 3EHY |
| Descriptor | Macrophage metalloelastase, ZINC ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | matrix metalloproteinase, mmp12, elastase, complex (elastase-inhibitor), metallo elastase, calcium, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P39900 |
| Total number of polymer chains | 1 |
| Total formula weight | 18082.96 |
| Authors | Calderone, V. (deposition date: 2008-09-15, release date: 2009-05-19, Last modification date: 2023-11-01) |
| Primary citation | Dragoni, E.,Calderone, V.,Fragai, M.,Jaiswal, R.,Luchinat, C.,Nativi, C. Biotin-tagged probes for MMP expression and activation: design, synthesis, and binding properties Bioconjug.Chem., 20:719-727, 2009 Cited by PubMed Abstract: The design and synthesis of biotin chain-terminated inhibitors (BTI) showing high affinity for matrix metalloproteinases (MMPs) on one side and high affinity for avidin through the biotinylated tag on the other are reported. The affinity of the designed BTI toward five different MMPs has been evaluated and the simultaneous formation of a highly stable ternary system Avidin-BTI-MMP clearly assessed. This system will permit the development of new approaches to detect, quantify, or collect MMPs in biological samples, with potential applications in vivo. PubMed: 19275207DOI: 10.1021/bc8003827 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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