Protein Dimer Structure with Cysteine Residues - Molecular Visualization #1262463 (License: Personal Use)

This high-resolution molecular visualization depicts a homodimeric protein structure, where Monomer A (yellow) and Monomer B (purple) form symmetric subunits connected via interchain interactions. Key functional residues-including Cys220A, Cys220B, Cys350A, and Cys350B-are highlighted in green, indicating potential disulfide bridges, while red clusters represent active or binding sites. The N-termini are marked, and the overall fold includes α-helices and β-sheets typical of globular enzymes or receptors.

Used in academic publications, educational resources, and bioinformatics platforms to illustrate protein quaternary structure, cysteine-mediated stabilization, and structure-function relationships; targets researchers, students, and clinicians studying enzyme mechanisms or drug design.