220.127.116.11: N-carbamoylsarcosine amidase
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amidase, carbamoylsarcosine, CSHase, N-carbamoylsarcosine amidohydrolase, N-carbamoylsarcosine amidase Ta0454
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Crystallization on EC 18.104.22.168 - N-carbamoylsarcosine amidase
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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