EC Number   |
|---|
   3.1.1.101 | 0.92 A resolution X-ray crystal structure reveals features common to both cutinases and lipases. PETase retains the ancestral alpha/beta-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases |
| 3.1.1.101 | hanging-drop vapor-diffusion technique at 20°C. Crystal structure of PETase at 1.5 A resolution. The enzyme has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested |
| 3.1.1.101 | molecular replacement with a poly-Ala model of Streptomyces exofoliatus lipase, PDB-ID: 1JFR, in free as well as in inhibitor-bound form. The enzyme forms a classical alpha/beta-hydrolase fold with a central nine-stranded beta-sheet flanked by 11 alpha-helices on both sides. The catalytic triad, comprising S130, D176 and H208, is located in a crevice on the surface of the enzyme |
| 3.1.1.101 | sitting drop vapor diffusion method at 4°C with a mixture at a 1:1 ratio of protein and reservoir solution. Crystal structure of PETase is determined at 2.02 A resolution and employed in molecular dynamics simulations showing that the active site of PETase has higher flexibility at room temperature than its thermophilic counterparts. This flexibility is controlled by a novel disulfide bond in its active site, with its removal leading to destabilization of the catalytic triad and reduction of the hydrolase activity. High flexibility of PETase loops at room temperature enables this enzyme to bind and degrade PET more efficiently than other cutinases |
| 3.1.1.101 | sitting-drop vapor-diffusion method at 25°C, crystallized in the orthorhombic space group P212121. The structure is solved at 1.58 A resolution |
| 3.1.1.101 | structural model generated on the basis of PDB ID 3VIS. The polyester hydrolase reveals a typical alpha/beta hydrolase fold. The catalytic triad formed by residues S130, D176 and H208 is exposed to the solvent |
