3znb

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spinqualitylabelsall models 3znb, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

METALLO-BETA-LACTAMASE (ZN, HG-BOUND FORM)

Overview

The metallo-beta-lactamases require zinc or cadmium for hydrolyzing, beta-lactam antibiotics and are inhibited by mercurial compounds. To data, there are no clinically useful inhibitors of this class of enzymes. The, crystal structure of the Zn(2+)-bound enzyme from Bacteroides fragilis, contains a binuclear zinc center in the active site. A hydroxide, coordinated to both zinc atoms, is proposed as the moiety that mounts the, nucleophilic attack on the carbonyl carbon atom of the beta-lactam ring., To study the metal coordination further, the crystal structures of a, Cd(2+)-bound enzyme and of an Hg(2+)-soaked zinc-containing enzyme have, been determined at 2.1 A and 2.7 A, respectively. Given the diffraction, resolution, the Cd(2+)-bound enzyme exhibits the same active-site, architecture ... [(full description)]

About this Structure

3ZNB is a [Single protein] structure of sequence from [Bacteroides fragilis] with ZN, HG and NA as [ligands]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis., Concha NO, Rasmussen BA, Bush K, Herzberg O, Protein Sci. 1997 Dec;6(12):2671-6. PMID:9416622

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