Fig. 9
From: Stability and functional consequences of disulfide bond engineering in Aspergillus flavus uricase
Tunnel visualization and profile to the active site in uricase muteins. The tunnel profile provides insights into the potential accessibility of the active site and any potential bottlenecks or constrictions introduced by the mutations. The left panel shows the enzyme structure with a transparent surface representation. The backbone is rendered as gray cartoon ribbons, indicating secondary structures. Cysteine residues involved in disulfide bonding are highlighted in yellow, with corresponding bonds displayed as yellow sticks. The active site tunnel is visualized as a green surface. The right panel presents a profile of tunnel radii along their depths, with the x-axis representing tunnel depth and the y-axis the tunnel radius in Ångströms. The tunnel profile provides insights into the potential accessibility of the active site and any potential bottlenecks or constrictions introduced by the mutations. Image created using PyMOL version 3.0.0.
