3lka | pdb_00003lka

Catalytic domain of human MMP-12 complexed with hydroxamic acid and paramethoxy-sulfonyl amide

spinqualitylabelsall models 3lka, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lka is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, HAE, M4S, ZN Gene: HME, MMP12 (Homo sapiens) Activity: Macrophage elastase, with EC number 3.4.24.65 Resources: FirstGlance, OCA, RCSB, PDBsum 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 For several drug leads obtained by tethering weak binding ligands, the dissociation constant is smaller than the product of those of the individual fragments by a factor named the linking coefficient, E. This favorable contribution is attributed to the entropic gain that is realized when two weak binding ligands are tethered. Here we show a case study where the linking coefficient is strikingly small (E = 2.1 x 10(-3) M(-1)) and its totally entropic nature is demonstrated. Entropic Contribution to the Linking Coefficient in Fragment Based Drug Design: A Case Study.,Borsi V, Calderone V, Fragai M, Luchinat C, Sarti N J Med Chem. 2010 Apr 23. PMID:20415416 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-2 microglobulin Major histocompatibility complex Matrix metalloproteinase

Proteopedia Page Contributors and Editors (what is this?)

OCA