Cystathionine <b><i>β</i></b>-Lyase-Like Protein with Pyridoxal Binding Domain Characterized in <i>Leishmania major</i> by Comparative Sequence Analysis and Homology Modelling

<table class="table-group" width="800px"><tr class="fig-image" id="a"><td><img alt="520435.fig.003a" src="https://static.hindawi.com/articles/isrn/volume-2013/520435/figures/520435.fig.003a.jpg"/></td></tr><tr class="fig-caption"><td align="center"><table><tr><td><b>(a) </b>CBLP homology model </td></tr></table></td></tr><tr class="fig-image" id="b"><td><img alt="520435.fig.003b" src="https://static.hindawi.com/articles/isrn/volume-2013/520435/figures/520435.fig.003b.jpg"/></td></tr><tr class="fig-caption"><td align="center"><table><tr><td><b>(b) </b>Template (CBL of <i>A. thaliana</i>) </td></tr></table></td></tr></table>

<table>Comparative protein structure analysis (ProSA) calculates <i>Z</i>-score for (a) CBLP homology model, (b) template (cystathionine <i><i>β</i></i>-lyase of <i>Arabidopsis thaliana</i>).</table>

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Figure 3

Figure 3: Cystathionine <b><i>β</i></b>-Lyase-Like Protein with Pyridoxal Binding Domain Characterized in <i>Leishmania major</i> by Comparative Sequence Analysis and Homology Modelling 

Figure 3 | Cystathionine β-Lyase-Like Protein with Pyridoxal Binding Domain Characterized in Leishmania major by Comparative Sequence Analysis and Homology Modelling 