Crystal Structural and Functional Analysis of the Putative Dipeptidase from <i>Pyrococcus horikoshii</i> OT3

<table>Deviations of C<svg height="7.9499998" id="M125" style="vertical-align:-0.1638pt" version="1.1" viewbox="0 0 9.7749996 7.9499998" width="9.7749996" xmlns="http://www.w3.org/2000/svg" xmlns:xlink="http://www.w3.org/1999/xlink">
<g transform="matrix(.017,-0,0,-.017,.062,7.675)"><path d="M545 106q-67 -118 -134 -118q-24 0 -40 37.5t-30 129.5h-2q-47 -72 -103 -119.5t-108 -47.5q-47 0 -76 45.5t-29 119.5q0 113 85 204t174 91q47 0 70 -33.5t43 -119.5h3q32 47 80 140l55 13l10 -9q-47 -80 -138 -201q17 -99 27.5 -136t22.5 -37q23 0 69 61zM333 204
q-14 98 -31 149.5t-50 51.5q-49 0 -94 -70t-45 -164q0 -55 15.5 -86t40.5 -31q70 0 164 150z" id="x1D6FC"></path></g>
</svg> atoms after the C<svg height="7.9499998" id="M126" style="vertical-align:-0.1638pt" version="1.1" viewbox="0 0 9.7749996 7.9499998" width="9.7749996" xmlns="http://www.w3.org/2000/svg" xmlns:xlink="http://www.w3.org/1999/xlink">
<g transform="matrix(.017,-0,0,-.017,.062,7.675)"><path d="M545 106q-67 -118 -134 -118q-24 0 -40 37.5t-30 129.5h-2q-47 -72 -103 -119.5t-108 -47.5q-47 0 -76 45.5t-29 119.5q0 113 85 204t174 91q47 0 70 -33.5t43 -119.5h3q32 47 80 140l55 13l10 -9q-47 -80 -138 -201q17 -99 27.5 -136t22.5 -37q23 0 69 61zM333 204
q-14 98 -31 149.5t-50 51.5q-49 0 -94 -70t-45 -164q0 -55 15.5 -86t40.5 -31q70 0 164 150z" id="x1D6FC"></path></g>
</svg> superposition between <i>Ph </i>dpd and Zn-<i>Ph</i>dpd. Downward and upward arrows represent the positions of H198, D215, D226, H290, E319, and E333 which are important residues in the active site.</table>

Journal of Biophysics

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Figure 6

Figure 6: Crystal Structural and Functional Analysis of the Putative Dipeptidase from <i>Pyrococcus horikoshii</i> OT3 

Journal of Biophysics

Crystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3

Figure 6