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Acyl pocket binding site

Sequence Peripheral site Choline binding site Acyl pocket ... [Pg.177]

Comparison of the KS binding sites from homology models tallies well with the experimental data for these KS domains. In order to test the hypothesis that a bulky residue at the X-Cys position precludes acylation by fl-carbon branched substrates, a M237A mutant was proposed. Simple alteration to the homology model suggested that a Met to Ala mutation would indeed provide additional space in the binding pocket for a f)-branched substrate (Fig. 3.9). [Pg.81]


See other pages where Acyl pocket binding site is mentioned: [Pg.195]    [Pg.245]    [Pg.89]    [Pg.393]    [Pg.106]    [Pg.614]    [Pg.378]    [Pg.103]    [Pg.266]    [Pg.268]    [Pg.691]    [Pg.2051]    [Pg.243]    [Pg.403]    [Pg.265]    [Pg.108]    [Pg.362]    [Pg.362]    [Pg.89]    [Pg.844]    [Pg.298]    [Pg.359]    [Pg.365]    [Pg.457]    [Pg.457]    [Pg.126]    [Pg.176]    [Pg.351]    [Pg.115]    [Pg.403]    [Pg.17]    [Pg.161]    [Pg.7]    [Pg.42]    [Pg.82]    [Pg.85]    [Pg.762]    [Pg.517]    [Pg.358]    [Pg.51]    [Pg.170]    [Pg.101]   


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Acylation site

Binding pocket

Binding site pocket

POCKET

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