    3.5.1.59 | structure solved and refined at a resolution of 2.35 A. The enzyme shares a similar fold and a highly conserved C-D-K-catalytic triad, Cys123, Asp9, and Lys90 with the structures of three cysteine hydrolases (PDB codes: 1NBA, 1IM5, and 2HOR). Molecular dynamics simulations of Ta0454/N-carbamoylsarcosine and Ta0454/pyrazinamide complexes are performed to determine the structural basis of the substrate binding pattern for each ligand. The predicted binding free energies suggest that Ta0454 is selective for N-carbamoylsarcosine over pyrazinamide, and zinc ions play an important role in the favorable substrate bound states |
