1jud

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1jud, resolution 2.5Å

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L-2-HALOACID DEHALOGENASE

Overview

L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of, L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic, acids. The crystal structure of the homodimeric enzyme from Pseudomonas, sp. YL has been determined by a multiple isomorphous replacement method, and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%., The subunit consists of two structurally distinct domains: the core domain, and the subdomain. The core domain has an alpha/beta structure formed by a, six-stranded parallel beta-sheet flanked by five alpha-helices. The, subdomain inserted into the core domain has a four helix bundle structure, providing the greater part of the interface for dimer formation. There is, an active site cavity between the domains. An experimentally ... [(full description)]

About this Structure

1JUD is a [Single protein] structure of sequence from [Pseudomonas]. Active as [[1]], with EC number [3.8.1.2]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold., Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K, J Biol Chem. 1996 Aug 23;271(34):20322-30. PMID:8702766

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