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TitleThe catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 3587-3596, Year 2011
Publish dateOct 12, 2010 (structure data deposition date)
AuthorsWahlgren, W.Y. / Pal, G. / Kardos, J. / Porrogi, P. / Szenthe, B. / Patthy, A. / Graf, L. / Katona, G.
External linksJ. Biol. Chem. / PubMed:21097875
MethodsX-ray diffraction
Resolution0.93 Å
Structure data

PDB-2xtt:
Bovine trypsin in complex with evolutionary enhanced Schistocerca gregaria protease inhibitor 1 (SGPI-1-P02)
Method: X-RAY DIFFRACTION / Resolution: 0.93 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

Source
  • bos taurus (domestic cattle)
  • schistocerca gregaria (desert locust)
KeywordsHYDROLASE / CATALYTIC MECHANISM / INHIBITION / IN VITRO EVOLUTION

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