2uxy

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2uxy, resolution 1.25Å

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ALIPHATIC AMIDASE

Overview

Microbial amidases belong to the thiol nitrilases family and have, potential biotechnological applications in chemical and pharmaceutical, industries as well as in bioremediation. The amidase from Pseudomonas, aeruginosa isa6 x 38-kDa enzyme that catalyzes the hydrolysis of a small, range of short aliphatic amides. The hereby reported high resolution, crystallographic structure shows that each amidase monomer is formed by a, globular four-layer alphabetabetaalpha sandwich domain with an additional, 81-residue long C-terminal segment. This wraps arm-in-arm with a, homologous C-terminal chain of another monomer, producing a strongly, packed dimer. In the crystal, the biological active homo-hexameric amidase, is built grouping three such dimers around a crystallographic 3-fold axis., The ... [(full description)]

About this Structure

2UXY is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with SO4 as [ligand]. Active as [Amidase], with EC number [3.5.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state., Andrade J, Karmali A, Carrondo MA, Frazao C, J Biol Chem. 2007 Jul 6;282(27):19598-605. Epub 2007 Apr 17. PMID:17442671

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