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TitleCanonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases
Journal, issue, pagesJ. Biol. Chem., Vol. 278, Page 37881-37887, Year 2003
Publish dateMar 3, 2003 (structure data deposition date)
AuthorsDementiev, A. / Simonovic, M. / Volz, K. / Gettins, P.G.
External linksJ. Biol. Chem. / PubMed:12860985
MethodsX-ray diffraction
Resolution2.3 - 2.65 Å
Structure data

PDB-1oo8:
CRYSTAL STRUCTURE OF A1PI-PITTSBURGH IN THE NATIVE CONFORMATION
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-1oph:
NON-COVALENT COMPLEX BETWEEN ALPHA-1-PI-PITTSBURGH AND S195A TRYPSIN
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • bos taurus (cattle)
KeywordsHYDROLASE INHIBITOR / SERPIN / PITTSBURGH VARIANT / HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEINASE INHIBITOR / MICHAELIS-LIKE COMPLEX / ALPHA-1 ANTITRYPSIN / TRYPSIN / HYDROLASE-HYDROLASE INHIBITOR COMPLEX

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