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
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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 Descriptor: ACETYL GROUP, N-[(BENZYLOXY)CARBONYL]-L-ALANINE, PHENYLALANINE AMIDE, ... Authors: Yin, J, Bergmann, E.M, Cherney, M.M, Lall, M.S, Jain, R.P, Vederas, J.C, James, M.N.G. Deposit date: 2005-06-29 Release date: 2005-12-27 Last modified: 2021-11-10 Method: X-RAY DIFFRACTION (1.55 Å) Cite: Dual 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 J.MOL.BIOL., 354, 2005
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2005-06-29



