1EPT

REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN

Summary for 1EPT

• Entry DOI: 10.2210/pdb1ept/pdb
• Descriptor: PORCINE E-TRYPSIN, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: hydrolase (serine protease)
• Biological source: Sus scrofa (pig); More
• Cellular location: Secreted, extracellular space: P00761 P00761 P00761
• Total number of polymer chains: 3
• Total formula weight: 23567.61

Authors

Huang, Q.,Wang, Z.,Li, Y.,Liu, S.,Tang, Y. (deposition date: 1994-06-07, release date: 1995-02-07, Last modification date: 2024-06-05)

Primary citation

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, 1209:77-82, 1994

PubMed Abstract: 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.

PubMed: 7947985
DOI: 10.1016/0167-4838(94)90139-2

Experimental method

X-RAY DIFFRACTION (1.8 Å)