3SK0
structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant DhaA12
Summary for 3SK0
| Entry DOI | 10.2210/pdb3sk0/pdb |
| Related | 1BN6 1CQW |
| Descriptor | Haloalkane dehalogenase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | catalytic pentad, alpha/beta-hydrolase fold, hydrolase, halide binding, hydrolytic dehalogenation |
| Biological source | Rhodococcus rhodochrous |
| Total number of polymer chains | 1 |
| Total formula weight | 35432.50 |
| Authors | Lahoda, M.,Stsiapanava, A.,Mesters, J.,Koudelakova, T.,Damborsky, J.,Kuta-Smatanova, I. (deposition date: 2011-06-22, release date: 2012-06-27, Last modification date: 2023-09-13) |
| Primary citation | Sykora, J.,Brezovsky, J.,Koudelakova, T.,Lahoda, M.,Fortova, A.,Chernovets, T.,Chaloupkova, R.,Stepankova, V.,Prokop, Z.,Smatanova, I.K.,Hof, M.,Damborsky, J. Dynamics and hydration explain failed functional transformation in dehalogenase design. Nat.Chem.Biol., 10:428-430, 2014 Cited by PubMed Abstract: We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase. PubMed: 24727901DOI: 10.1038/nchembio.1502 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
Download full validation report
