5EH9
Indirect contributions of mutations underlie optimization of new enzyme function
Summary for 5EH9
Entry DOI | 10.2210/pdb5eh9/pdb |
Related | 3DHB |
Descriptor | N-acyl homoserine lactonase AiiA, ZINC ION, GLYCEROL, ... (5 entities in total) |
Functional Keywords | n-acyl homoserine lactonase from bacillus thuringiensis, hydrolase |
Biological source | Bacillus thuringiensis subsp. kurstaki |
Total number of polymer chains | 1 |
Total formula weight | 29432.14 |
Authors | Hong, N.-S.,Jackson, C.J.,Tokuriki, N.,Yang, G.,Baier, F. (deposition date: 2015-10-28, release date: 2016-09-07, Last modification date: 2023-09-27) |
Primary citation | Yang, G.,Hong, N.,Baier, F.,Jackson, C.J.,Tokuriki, N. Conformational Tinkering Drives Evolution of a Promiscuous Activity through Indirect Mutational Effects. Biochemistry, 55:4583-4593, 2016 Cited by PubMed: 27444875DOI: 10.1021/acs.biochem.6b00561 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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