Phanerochaete chrysosporium (Pc), is a prominent lignin-degrading fungus which serves as an important source for lignin-degrading enzymes (LDEs). The present study was focused on a detailed in silico analysis and gene expression patterns of lignin peroxidases (PcLiPs), which is a significant class of LDEs. In spite of extensive research on P. chrysosporium enzymes, the number of PcLiP isozymes remains unexplored. In the present study, ten PcLiP sequences were identified by the RedoXiBase and BLAST survey, displaying putative glycosylated extracellular protein which was approximately 38 to 39 kDa. Different domains of the protein included putative binding sites for stress, nutrient components, metal ions, peroxidase motifs, ligninase motifs, and also secretory signal peptides. Molecular docking analysis of all the PcLiPs, showed that the PcLiP4 had strong binding affinity towards hydrogen peroxide (H