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(D ) Detailed TBCC-Arl2 interface model showing catalytic role of Arg186 (Arg finger) and selectivity role of Phe233 and Phe235.
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Fe66.3B16.6Y17.1 amorphous structures designed based on a competitive atomic cluster model shows excellent catalytic ability due to the competition between two different Fe-rich clusters Fe11Y3 and Fe8B2.
c The refined structure of RrQR by an energy minimization (red) is superimposed on the structure of the catalytic model shown in Figure 4a (blue).
A simple catalytic model showed that seroconversion and seroreversion rates were highly age-dependent.
Also, it shows catalytic effects [230].
Consequently, isolated catalytic domains should show catalytic turnover comparable to that of activated sGC.
Generally, α-esterases contain the conserved catalytic triad and showed catalytic function.
Compared to the template the AnMan5B model showed an overall well-conserved catalytic site with no apparent differences in subsites −2 and −1 (data not shown).
The model showed an overall well-conserved catalytic site compared to the template structure TrMan5A, with the only notable difference seen on the aglycone side where AnMan5B had a tryptophan (Trp242) instead of a leucine in the template (Fig. 6).
The model shows changes in the proportion of free catalytic subunits of PKA when cAMP is set to low (C low ) and high (C high ) levels.
The model shows the TBCC loop resides above Arl2 during the catalytic interface.
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