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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Huang Q, Wang Z, Li Y, Liu S, Tang Y. Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin. Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985
