2d1o
Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]
About this StructureAbout this Structure
2D1O is a Single protein structure of sequence from Homo sapiens with ZN, CA and FA4 as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453., Kohno T, Hochigai H, Yamashita E, Tsukihara T, Kanaoka M, Biochem Biophys Res Commun. 2006 May 26;344(1):315-22. Epub 2006 Mar 27. PMID:16603129
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