1gkp

From Proteopedia

Revision as of 06:23, 30 October 2007

D-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM THERMUS SP. IN SPACE GROUP C2221

Overview

Dihydropyrimidinases (hydantoinases) catalyse the reversible hydrolytic, ring-opening of cyclic diamides such as dihydropyrimidines in the, catabolism of pyrimidines. In biotechnology, these enzymes find, application in the enantiospecific production of amino acids from racemic, hydantoins. The crystal structure of a D-enantio-specific, dihydropyrimidinase from Thermus sp. (D-hydantoinase) was solved de novo, by multiwavelength anomalous diffraction phasing. In spite of a large unit, cell the D-hydantoinase crystals exhibit excellent diffraction properties., The structure was subsequently refined at 1.30 A resolution against native, data. The core of D-hydantoinase consists of a (alpha/beta)(8)-barrel, which is flanked by a beta-sheet domain and some additional helices. In, the active ... [(full description)]

About this Structure

1GKP is a [Single protein] structure of sequence from [Thermus sp.] with ZN, SO4 and EPE as [ligands]. Active as [Hydrolase], with EC number [3.5.2.2]. Structure known Active Site: ASA. Full crystallographic information is available from [OCA].

Reference

X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 A resolution., Abendroth J, Niefind K, Schomburg D, J Mol Biol. 2002 Jun 28;320(1):143-56. PMID:12079340

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