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TitleComparison of Anionic and Cationic Trypsinogens: The Anionic Activation Domain is More Flexible in Solution and Differs in its Mode of Bpti Binding in the Crystal Structure
Journal, issue, pagesProtein Sci., Vol. 8, Page 253-258, Year 1999
Publish dateJul 15, 1998 (structure data deposition date)
AuthorsPasternak, A. / Ringe, D. / Hedstrom, L.
External linksPubMed:10210204
MethodsX-ray diffraction
Resolution1.8 - 2.2 Å
Structure data

PDB-3tgi:
WILD-TYPE RAT ANIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3tgj:
S195A TRYPSINOGEN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
  • bos taurus (domestic cattle)
KeywordsCOMPLEX (SERINE PROTEASE/INHIBITOR) / COMPLEX (SERINE PROTEASE-INHIBITOR) / COMPLEX (SERINE PROTEASE-INHIBITOR) complex

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