8IBM
Sulfate bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation
Summary for 8IBM
Entry DOI | 10.2210/pdb8ibm/pdb |
Descriptor | Alpha/beta hydrolase family protein, CALCIUM ION, SULFATE ION, ... (4 entities in total) |
Functional Keywords | protein engineering, polyesterase, disulfide bond, metal binding, ligand complex, hydrolase |
Biological source | Saccharomonospora viridis |
Total number of polymer chains | 2 |
Total formula weight | 58051.36 |
Authors | Emori, M.,Numoto, N.,Kamiya, N.,Oda, M. (deposition date: 2023-02-10, release date: 2023-03-15, Last modification date: 2024-10-23) |
Primary citation | Numoto, N.,Kamiya, N.,Oda, M. Improvement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism. Biorxiv, 2023 Cited by DOI: 10.1101/2023.02.26.529345PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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