8OZV

Imine Reductase from Ajellomyces dermatitidis in complex with 2,2-difluoroacetophenone

8OZV の概要

• エントリーDOI: 10.2210/pdb8ozv/pdb
• 分子名称: Oxidoreductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 2,2-bis(fluoranyl)-1-phenyl-ethanone, ... (4 entities in total)
• 機能のキーワード: imine reductase, amine, dehydrogenase, nadp, oxidoreductase
• 由来する生物種: Blastomyces dermatitidis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31030.12

構造登録者

Sharma, M.,Grogan, G. (登録日: 2023-05-09, 公開日: 2023-08-30, 最終更新日: 2023-09-13)

主引用文献

Sharma, M.,Cuetos, A.,Willliams, A.,Gonzalez-Martinez, D.,Grogan, G.
Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms.
Acta Crystallogr.,Sect.F, 79:224-230, 2023

PubMed Abstract: 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 P321 and was refined to 2.01 Å resolution, features two molecules (one dimer) in the asymmetric unit in complex with the redox-inactive cofactor NADPH. The second form, which belongs to space group C2 and was refined to 1.73 Å 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 P321 and was refined to 1.52 Å 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.

PubMed: 37581897
DOI: 10.1107/S2053230X23006672

実験手法

X-RAY DIFFRACTION (1.52 Å)