Enzyme catalyzed biosynthesis of steroidal drugs is an important process for pharmaceutical manufacturing. Cytochrome P450 (P450) monooxygenases are important for hydroxylation of steroid structures because they can catalyze the oxidation of inactive carbon bonds with high selectivity and efficiency. CYP119 is an acidothermophilic P450 from Sulfolobus acidocaldarius, which has the potential to be used as biocatalyst for industrial production since it shows activity at high temperature and low pH conditions. In this work we aim to use CYP119 for selective hydroxylation of progesterone, which is not the original substrate of CYP119, for production of precursor molecules of important hormones like cortisone and aldosterone. Crystal structure of CYP119 (PDB ID: 1F4T) was used for selecting residues that were mutated according to structural alignment with other CYPs that can catalyze progesterone hydroxylation naturally. Progesterone-docking performed with CYP119 to identify residues that create clashes with substrate. Finally selected 12 residues (Leu69, Val151, Phe153, Leu155, Leu205, Ile208, Ala209, Thr213, Thr214, Val254, Thr257, Leu354) were mutated with PyRosetta program to Gly, Glu, Phe, Met, Ala, His, Arg and Ile. Progesterone-docking performed with using DockMCM Protocol of PyRosetta. We used two different starting coordinates of progesterone for docking and results were eliminated according to their energy scores. Best mutants were used for creating double/triple mutants and second round of docking and elimination process were performed with using double/triple mutant enzymes. Final number of 11 mutants with best scores were selected and their possible products were identified.