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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 DOI10.2210/pdb8ibm/pdb
DescriptorAlpha/beta hydrolase family protein, CALCIUM ION, SULFATE ION, ... (4 entities in total)
Functional Keywordsprotein engineering, polyesterase, disulfide bond, metal binding, ligand complex, hydrolase
Biological sourceSaccharomonospora viridis
Total number of polymer chains2
Total formula weight58051.36
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 citationNumoto, 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: 10.1101/2023.02.26.529345
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

227111

数据于2024-11-06公开中

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