2qn5

Crystal Structure and Functional Study of the Bowman-Birk Inhibitor from Rice Bran in Complex with Bovine TrypsinCrystal Structure and Functional Study of the Bowman-Birk Inhibitor from Rice Bran in Complex with Bovine Trypsin

Structural highlights 2qn5 is a 2 chain structure with sequence from Bos taurus and Oryza sativa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1c2a, 1tx6, 1k9b, 1s0q Activity: Trypsin, with EC number 3.4.21.4 Resources: FirstGlance, OCA, PDBe, 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 Bowman-Birk inhibitors (BBIs) are cysteine-rich proteins with inhibitory activity against proteases that are widely distributed in monocot and dicot species. The expression of rice BBI from Oryza sativa is up-regulated and induced by pathogens or insects during germination of rice seeds. The rice BBI (RBTI) of molecular weight 15 kDa has been crystallized using the hanging-drop vapour-diffusion method. According to the diffraction of rice BBI crystals at a resolution of 2.07 A, the unit cell belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 74.37, b = 96.69, c = 100.36 A. Preliminary analysis indicates four BBI molecules in an asymmetric unit, with a solvent content of 58.29%. Purification, crystallization and preliminary X-ray crystallographic analysis of rice Bowman-Birk inhibitor from Oryza sativa.,Lin YH, Li HT, Huang YC, Hsieh YC, Guan HH, Liu MY, Chang T, Wang AH, Chen CJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):522-4. Epub 2006 May 5. PMID:16754971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin Trypsin inhibitor

spinqualitylabelsall models 2qn5, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image