9DEH
The designed serine hydrolase known as win31
Summary for 9DEH
| Entry DOI | 10.2210/pdb9deh/pdb |
| Descriptor | Win31, TETRAETHYLENE GLYCOL, L(+)-TARTARIC ACID, ... (4 entities in total) |
| Functional Keywords | serine hydrolase, designed enzyme, helical, lit, hydrolase |
| Biological source | synthetic construct |
| Total number of polymer chains | 5 |
| Total formula weight | 91861.04 |
| Authors | Pellock, S.J.,Lauko, A.,Bera, A.K. (deposition date: 2024-08-28, release date: 2025-02-19, Last modification date: 2025-04-30) |
| Primary citation | Lauko, A.,Pellock, S.J.,Sumida, K.H.,Anishchenko, I.,Juergens, D.,Ahern, W.,Jeung, J.,Shida, A.F.,Hunt, A.,Kalvet, I.,Norn, C.,Humphreys, I.R.,Jamieson, C.,Krishna, R.,Kipnis, Y.,Kang, A.,Brackenbrough, E.,Bera, A.K.,Sankaran, B.,Houk, K.N.,Baker, D. Computational design of serine hydrolases. Science, 388:eadu2454-eadu2454, 2025 Cited by PubMed Abstract: The design of enzymes with complex active sites that mediate multistep reactions remains an outstanding challenge. With serine hydrolases as a model system, we combined the generative capabilities of RFdiffusion with an ensemble generation method for assessing active site preorganization to design enzymes starting from minimal active site descriptions. Experimental characterization revealed catalytic efficiencies (/) up to 2.2x10 M s and crystal structures that closely match the design models (Cα RMSDs < 1 Å). Selection for structural compatibility across the reaction coordinate enabled identification of new catalysts in low-throughput screens with five different folds distinct from those of natural serine hydrolases. Our de novo approach provides insight into the geometric basis of catalysis and a roadmap for designing enzymes that catalyze multistep transformations. PubMed: 39946508DOI: 10.1126/science.adu2454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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