6l2e | pdb_00006l2e

Crystal structure of a cupin protein (tm1459, H52A mutant) in copper (Cu) substituted form

spinqualitylabelsall models 6l2e, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l2e is a 2 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.201Å Ligands: CSD, CU, MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9X1H0_THEMA Publication Abstract from PubMed Cupin superfamily proteins (TM1459) work as a macromolecular ligand framework with a double-stranded beta-barrel structure ligating to a Cu ion through histidine side chains. Variegating the first coordination sphere of TM1459 revealed that H52A and H54A/H58A mutants effectively catalyzed the diastereo- and enantioselective Michael addition reaction of nitroalkanes to an alpha,beta-unsaturated ketone. Moreover, calculated substrate docking signified C106N and F104W single-point mutations, which inverted the diastereoselectivity of H52A and further improved the stereoselectivity of H54A/H58A, respectively. Cupin Variants as a Macromolecular Ligand Library for Stereoselective Michael Addition of Nitroalkanes.,Fujieda N, Ichihashi H, Yuasa M, Nishikawa Y, Kurisu G, Itoh S Angew Chem Int Ed Engl. 2020 Feb 19. doi: 10.1002/anie.202000129. PMID:32073197 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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