1sbw

CRYSTAL STRUCTURE OF MUNG BEAN INHIBITOR LYSINE ACTIVE FRAGMENT COMPLEX WITH BOVINE BETA-TRYPSIN AT 1.8A RESOLUTION

spinqualitylabelsall models 1sbw, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sbw is a 2 chain structure with sequence from Bos taurus and Vigna radiata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRY1_BOVIN 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 crystal structure of the complex of mung bean inhibitor lysine active fragment with bovine beta-trypsin has been determined by X-ray crystallographic analysis at a resolution of 1.8 A. Refinement of the model of the complex converged at a final R value of 0.16. From the resulting electron density map, about one-third of the residues of the inhibitor were identified and two residues, at position P4 and P2' respectively, were found to be inconsistent with the sequence reported previously. The peptide chain of the inhibitor at the trypsin active site turns back sharply at Pro23I and forms a 9-residue reactive loop, which interacts with trypsin in a similar manner to the other families of inhibitors, suggesting an important and common role of these regions in exhibiting inhibitory activity. Crystal structure of mung bean inhibitor lysine active fragment complex with bovine beta-trypsin at 1.8A resolution.,Zhu Y, Huang Q, Chi C J Biomol Struct Dyn. 1999 Jun;16(6):1219-24. PMID:10447205 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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