2D1O
Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor
Summary for 2D1O
| Entry DOI | 10.2210/pdb2d1o/pdb |
| Related | 2D1N |
| Descriptor | Stromelysin-1, ZINC ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | hydorolase metalloprotease, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P08254 |
| Total number of polymer chains | 2 |
| Total formula weight | 39799.99 |
| Authors | Kohno, T.,Hochigai, H.,Yamashita, E.,Tsukihara, T.,Kanaoka, M. (deposition date: 2005-08-30, release date: 2006-06-27, Last modification date: 2023-10-25) |
| Primary citation | Kohno, T.,Hochigai, H.,Yamashita, E.,Tsukihara, T.,Kanaoka, M. Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 Biochem.Biophys.Res.Commun., 344:315-322, 2006 Cited by PubMed Abstract: Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have been solved at 2.01 and 2.37A resolutions, respectively. The results revealed that the binding modes for this inhibitor to MMP-3 and -13 were quite similar. However, subtle comparative differences were observed at the bottom of S1' pockets, which were occupied with the guanidinomethyl moiety of the inhibitor. A remarkable feature of the inhibitor was the deep penetration of its long aliphatic chain into the S1' pocket and exposure of the guanidinomethyl moiety to the solvent. PubMed: 16603129DOI: 10.1016/j.bbrc.2006.03.098 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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