3I1C
Crystal Structure of a Novel Engineered Diels-Alderase: DA_20_00_A74I
Summary for 3I1C
| Entry DOI | 10.2210/pdb3i1c/pdb |
| Descriptor | Diisopropyl-fluorophosphatase, GLYCEROL (3 entities in total) |
| Functional Keywords | beta-propeller, hydrolase, metal-binding |
| Biological source | Loligo vulgaris (Common European squid) |
| Total number of polymer chains | 1 |
| Total formula weight | 36194.11 |
| Authors | Lambert, A.R.,Stoddard, B.L. (deposition date: 2009-06-26, release date: 2009-08-18, Last modification date: 2024-02-21) |
| Primary citation | Siegel, J.B.,Zanghellini, A.,Lovick, H.M.,Kiss, G.,Lambert, A.R.,St Clair, J.L.,Gallaher, J.L.,Hilvert, D.,Gelb, M.H.,Stoddard, B.L.,Houk, K.N.,Michael, F.E.,Baker, D. Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction. Science, 329:309-313, 2010 Cited by PubMed Abstract: The Diels-Alder reaction is a cornerstone in organic synthesis, forming two carbon-carbon bonds and up to four new stereogenic centers in one step. No naturally occurring enzymes have been shown to catalyze bimolecular Diels-Alder reactions. We describe the de novo computational design and experimental characterization of enzymes catalyzing a bimolecular Diels-Alder reaction with high stereoselectivity and substrate specificity. X-ray crystallography confirms that the structure matches the design for the most active of the enzymes, and binding site substitutions reprogram the substrate specificity. Designed stereoselective catalysts for carbon-carbon bond-forming reactions should be broadly useful in synthetic chemistry. PubMed: 20647463DOI: 10.1126/science.1190239 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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