4O5S
Crystal structure of Diels-Alderase CE11
Summary for 4O5S
Entry DOI | 10.2210/pdb4o5s/pdb |
Related | 1E1A 3I1C 3U0S 4O5T |
Descriptor | Diisopropyl-fluorophosphatase (2 entities in total) |
Functional Keywords | protein engineering, computer-aided design, diels-alder reaction, enzyme design, directed evolution, substrate specificity, beta-propeller, helix-loop-helix, de novo protein, artificial catalyst, diels-alderase, catalyst for cycloaddition, hydrolase |
Biological source | Loligo vulgaris (Common European squid) |
Total number of polymer chains | 2 |
Total formula weight | 74516.42 |
Authors | Beck, T.,Preiswerk, N.,Mayer, C.,Hilvert, D. (deposition date: 2013-12-20, release date: 2014-06-04, Last modification date: 2023-11-08) |
Primary citation | Preiswerk, N.,Beck, T.,Schulz, J.D.,Milovnik, P.,Mayer, C.,Siegel, J.B.,Baker, D.,Hilvert, D. Impact of scaffold rigidity on the design and evolution of an artificial Diels-Alderase. Proc.Natl.Acad.Sci.USA, 111:8013-8018, 2014 Cited by PubMed: 24847076DOI: 10.1073/pnas.1401073111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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