Glutaredoxin Protein Structure and Active Site Interaction Diagram #1404178 (License: Personal Use)

Panel A displays the tertiary structure of a glutaredoxin protein, highlighting its α-helices (red), β-sheets (green), and loop regions, with labeled termini (N-T, C-T) and glutathione (GS) binding pocket. Panel B provides an atomic-level view of the active site, illustrating hydrogen-bonding distances (3.5 Å and 5.1 Å) between serine residues S30 (yGrx1 and yGrx2 variants) and cysteine C27, crucial for enzymatic function in redox regulation.

Used in academic and biotech webpages explaining enzyme mechanisms, structural biology papers, or educational resources on redox proteins; targets researchers, students, and professionals seeking visual support for glutaredoxin function and active-site geometry.