Fig. 1
From: Unveiling the structure, function and dynamics of StmPr1 in Stenotrophomonas maltophilia virulence

Cartoon and topology plot of StmPr1 36 kDa. (a) The secondary structure, solved by X-ray crystallography, is indicated in different colors. Loops are depicted in green, sheets in yellow and helices in red. (b) The topology plot is depicted in the same color scheme and highlights the Ca-binding site and catalytic triad. (c) Top view of the secondary structure indicated in the same colors to show secondary structure features missing in a). The structure is rotated by 90° with the active site on top. Inserts 1–4 highlight relevant structural elements of StmPr1. The two disulfide bridges (Cys93-Cys141, 1 and Cys183 - Cys220, 3), the catalytic triad (2) and the calcium binding site (4) are highlighted in their own window.