1q3a

Crystal structure of the catalytic domain of human matrix metalloproteinase 10

spinqualitylabelsall models 1q3a, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1q3a is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, NGH, ZN Related: 1g49, 1bqo, 1d5j, 1d8f, 1uea Gene: MMP10 OR STMY2 (HUMAN) Activity: Stromelysin 2, with EC number 3.4.24.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MMP10_HUMAN] Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The catalytic domain of matrix metalloproteinase-10 (MMP-10) has been expressed in Escherichia coli and its crystal structure solved at 2.1 A resolution. The availability of this structure allowed us to critically examine the small differences existing between the catalytic domains of MMP-3 and MMP-10, which show the highest sequence identity among all MMPs. Furthermore, the binding mode of N-isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH), which is one of the most known commercial inhibitors of MMPs, is described for the first time. Crystal structure of the catalytic domain of human matrix metalloproteinase 10.,Bertini I, Calderone V, Fragai M, Luchinat C, Mangani S, Terni B J Mol Biol. 2004 Feb 20;336(3):707-16. PMID:15095982 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Matrix metalloproteinase

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