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1s6r
From Proteopedia
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| , resolution 2.24Å | |||||||
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| Ligands: | |||||||
| Activity: | Hydrolase, with EC number 3.5.2.6. | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
908R CLASS C BETA-LACTAMASE BOUND TO IODO-ACETAMIDO-PHENYL BORONIC ACID
Overview
The structures of the class C beta-lactamase from Enterobacter cloacae 908R alone and in complex with a boronic acid transition-state analogue were determined by X-ray crystallography at 2.1 and 2.3 A, respectively. The structure of the enzyme resembles those of other class C beta-lactamases. The structure of the complex with the transition-state analogue, iodo-acetamido-phenyl boronic acid, shows that the inhibitor is covalently bound to the active-site serine (Ser64). Binding of the inhibitor within the active site is compared with previously determined structures of complexes with other class C enzymes. The structure of the boronic acid adduct indicates ways to improve the affinity of this class of inhibitors. This structure of 908R class C beta-lactamase in complex with a transition-state analogue provides further insights into the mechanism of action of these hydrolases.
About this Structure
1S6R is a Single protein structure of sequence from Enterobacter cloacae. Full crystallographic information is available from OCA.
Reference
Crystal structure of Enterobacter cloacae 908R class C beta-lactamase bound to iodo-acetamido-phenyl boronic acid, a transition-state analogue., Wouters J, Fonze E, Vermeire M, Frere JM, Charlier P, Cell Mol Life Sci. 2003 Aug;60(8):1764-73. PMID:14521155
Page seeded by OCA on Thu Mar 20 14:01:11 2008
