8p2j | pdb_00008p2j

Imine Reductase from Ajellomyces dermatitidis in space group C21

spinqualitylabelsall models 8p2j, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8p2j is a 9 chain structure with sequence from Blastomyces dermatitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.73Å Ligands: NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A179UH34_BLAGS Publication Abstract from PubMed The NADPH-dependent imine reductase from Ajellomyces dermatitidis (AdRedAm) catalyzes the reductive amination of certain ketones with amine donors supplied in an equimolar ratio. The structure of AdRedAm has been determined in three forms. The first form, which belongs to space group P3(1)21 and was refined to 2.01 A resolution, features two molecules (one dimer) in the asymmetric unit in complex with the redox-inactive cofactor NADPH(4). The second form, which belongs to space group C2(1) and was refined to 1.73 A resolution, has nine molecules (four and a half dimers) in the asymmetric unit, each complexed with NADP(+). The third form, which belongs to space group P3(1)21 and was refined to 1.52 A resolution, has one molecule (one half-dimer) in the asymmetric unit. This structure was again complexed with NADP(+) and also with the substrate 2,2-difluoroacetophenone. The different data sets permit the analysis of AdRedAm in different conformational states and also reveal the molecular basis of stereoselectivity in the transformation of fluorinated acetophenone substrates by the enzyme. Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.,Sharma M, Cuetos A, Willliams A, Gonzalez-Martinez D, Grogan G Acta Crystallogr F Struct Biol Commun. 2023 Sep 1. doi: , 10.1107/S2053230X23006672. PMID:37581897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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