8pc7 | pdb_00008pc7

STRUCTURE OF ESTER-HYDROLASE EH3 FROM THE METAGENOME OF MARINE SEDIMENTS AT MILAZZO HARBOR (SICILY, ITALY) COMPLEXED WITH A DERIVATIVE OF BIPYRIDINE PHOSPHONATE

spinqualitylabelsall models 8pc7, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8pc7 is a 4 chain structure with sequence from Metagenome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: GOL, PEG, ZK8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2K8JN75_9BACT Publication Abstract from PubMed Metal complexes introduced into protein scaffolds can generate versatile biomimetic catalysts endowed with a variety of catalytic properties. Here, we synthesized and covalently bound a bipyridinyl derivative to the active centre of an esterase to generate a biomimetic catalyst that shows catecholase activity and enantioselective catalytic oxidation of (+)-catechin. Transforming an esterase into an enantioselective catecholase through bioconjugation of a versatile metal-chelating inhibitor.,Fernandez-Lopez L, Cea-Rama I, Alvarez-Malmagro J, Ressmann AK, Gonzalez-Alfonso JL, Coscolin C, Shahgaldian P, Plou FJ, Modregger J, Pita M, Sanz-Aparicio J, Ferrer M Chem Commun (Camb). 2023 Aug 1;59(62):9469-9472. doi: 10.1039/d3cc01946b. PMID:37376994 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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