Structural and functional evaluation of azo dye degrading enzymes were undertaken employing in silico analysis. 3D structure models for laccase (Q5EBY5) and hemeperoxidase (A0A1Q3E2I9) from the Lentinus sp. was generated using AlphaFold. Molecular docking was performed with AutoDock software for binding energy calculation, after identification of active site residues based on literature. Further, molecular dynamics simulation analysis was performed to evaluate the consistent binding of the dye molecules at the active site of the proteins. Molecular docking analysis revealed significant binding of three azo dyes, Amido Black 10B, Reactive Blue160, and Reactive Black 5 at the catalytic site of laccase (Q5EBY5) with significant binding energies of ？7.6 kcal/mol, ？7.4 kcal/mol and ？6.9 kcal/mol respectively indicating Q5EBY5 laccase as the competent enzyme for remediation of dyes. Further heme peroxidase (A0A1Q3E2I9) had shown higher negative binding energy of ？7.7 kcal/mol, ？6.4 kcal/mol for Amido Black 10B, Reactive Black 5, respectively. The number of hydrogen bonds in both the complexes between the protein and the ligand were consistent during the simulation and revealed effective interactions.
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