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Literature summary for 3.4.23.16 extracted from

  • Silva, A.M.; Cachau, R.E.; Sham, H.L.; Erickson, J.W.
    Inhibition and catalytic mechanism of HIV-1 aspartic protease (1996), J. Mol. Biol., 255, 321-346.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the structure of the HIV-1 protease in complex with A79285, a pseudo-C2 symmetric inhibitor, which contains a central difluoroketone motif determined with X-ray diffraction data extending to 1.7 A resolution. Crystals are grown at room temperature by hanging drop method with 37% w/v ammonium sulfate, 63 mM citrate and 126 mM sodium phosphate, pH 6.2 Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
A79285 a pseudo-C2 symmetric inhibitor, which contains a central difluoroketone motif Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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Reaction

Reaction Comment Organism Reaction ID
specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro proteolysis mechanism whereby only one active site Asp is initially protonated. The steps of this mechanism are: asymmetric binding of the substrate, hydration of the peptidic carbonyl by an active site water, proton translocation between the active site Asp residue simultaneously with carbonyl hydration Human immunodeficiency virus 1