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Protein Active Site Structural Comparison - Enzyme Residue Interactions #1404190 (License: Personal Use)
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Panel (a) illustrates a protein active site featuring residues N18, K68, N140, G20, L144, and F30 coordinated around a central water molecule (H₂O). Panel (b) shows a structurally similar but distinct conformation with residues D88, Y90, N147, H210, F101, and L214, also centered on a catalytic water molecule. Both models use color-coded ribbons and sticks to differentiate backbone, side chains, and ligands, supporting mechanistic enzymology studies.
Used in academic publications, biochemistry textbooks, or molecular modeling resources to explain enzyme catalysis, mutation effects, or structural dynamics; targets researchers, students, and educators seeking visual insight into active site architecture.
Related Cliparts: Detailed 3D structural models of enzyme active sites highlighting key amino acid residues (N18, G20, F30, etc.) and catalytic water molecules. Ideal for biochemistry research.
(view all Protein Active Site Structural Comparison - Enzyme Residue Interactions)
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