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Protein Structure with Critical Amino Acid Residues D261, M258, and S250 #1273773 (License: Personal Use)
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This high-resolution 3D ribbon model illustrates a protein’s secondary structural elements-including α-helices (pink, green) and β-sheets (beige)-with three critical amino acid side chains (Asp261, Met258, Ser250) emphasized as red spheres. The spatial arrangement suggests these residues may form part of an active site or allosteric regulatory region, commonly studied in enzymology and structural biology. Annotations indicate precise residue positions for functional interpretation.
Used in academic or biotech webpages explaining protein function, enzyme mechanisms, or disease-related mutations; targets researchers, students, and clinicians seeking structural insights into molecular pathology or drug design.
Related Cliparts: Visualize a 3D protein model showing functionally important residues D261, M258, and S250-essential for understanding enzyme active sites and mutation impacts.
(view all Protein Structure with Critical Amino Acid Residues D261, M258, and S250)
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