1ept

REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN

spinqualitylabelsall models 1ept, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ept is a 3 chain structure with sequence from Sus scrofa. 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 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TRYP_PIG 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 Porcine epsilon-trypsin is a three-chain inactivated trypsin from the limited autolysis of porcine beta-trypsin. It is cleaved at positions Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined by using the molecular replacement method, and refined at 1.8 A resolution. The R-value of final model is 0.184. Comparison with the electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and with that of native bovine beta-trypsin (HTNA), revealed no obvious changes except at the autolysis positions, and no changes at the active center were observed. The autolysis at positions Lys60-Ser61 and Lys145-Ser146 does not affect the conformation of His-57 in the active center and therefore cannot explain for a loss in porcine epsilon-trypsin activity. Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin.,Huang Q, Wang Z, Li Y, Liu S, Tang Y Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Trypsin 3D structures

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