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TitleDual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-derived beta-Lactone: Selective Crystallization and Formation of a Functional Catalytic Triad in the Active Site
Journal, issue, pagesJ. MOL. BIOL., Vol. 354, Page 854-871, Year 2005
Publish dateJun 29, 2005 (structure data deposition date)
AuthorsYin, J. / Bergmann, E.M. / Cherney, M.M. / Lall, M.S. / Jain, R.P. / Vederas, J.C. / James, M.N.G.
External linksJ. MOL. BIOL. / PubMed:16288920
MethodsX-ray diffraction
Resolution1.4 - 1.55 Å
Structure data

PDB-2a4o:
Dual modes of modification of Hepatitis A virus 3C protease by a serine derived beta-lactone: selective crytstallization and high resolution structure of the His102 adduct
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-2cxv:
Dual Modes of Modification of Hepatitis A Virus 3C Protease by a Serine-Derived betaLactone: Selective Crystallization and High-resolution Structure of the His-102 Adduct
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-BBL:
N-[(BENZYLOXY)CARBONYL]-L-ALANINE

ChemComp-ACE:
ACETYL GROUP

ChemComp-VAL:
VALINE

ChemComp-NFA:
PHENYLALANINE AMIDE

ChemComp-HOH:
WATER

Source
  • human hepatitis a virus hu/northern africa/mbb/1978
KeywordsHYDROLASE / beta barrel / Hepatitis A / picornavirus / 3C / cysteine protease / inhibitor / beta-Lactone

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