1okx

Binding Structure of Elastase Inhibitor Scyptolin A

spinqualitylabelsall models 1okx, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1okx is a 4 chain structure with sequence from Scytonema hofmannii and Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: 1BO, CNT, SUJ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CELA1_PIG Acts upon elastin. 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 Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.8 A resolution. The inhibitor occupies the most prominent subsites S1 through S4 of the elastase and prevents a hydrolytic attack by covering the active center with its rigid ring structure. The observed binding structure may help to design potent elastase inhibitors. Binding structure of elastase inhibitor scyptolin A.,Matern U, Schleberger C, Jelakovic S, Weckesser J, Schulz GE Chem Biol. 2003 Oct;10(10):997-1001. PMID:14583266 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elastase 3D structures

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