2rcx
From Proteopedia
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| - | [[Image:2rcx.gif|left|200px]] | + | [[Image:2rcx.gif|left|200px]] |
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| - | '''AmpC Beta-lactamase in complex with (1R)-1-(2-Thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)-phenyl) methylboronic acid''' | + | {{Structure |
| + | |PDB= 2rcx |SIZE=350|CAPTION= <scene name='initialview01'>2rcx</scene>, resolution 2.000Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=SM4:(1R)-1-(2-THIOPHEN-2-YL-ACETYLAMINO)-1-(3-(2-CARBOXYVINYL)-PHENYL) METHYLBORONIC ACID'>SM4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | ||
| + | |GENE= ampC, ampA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''AmpC Beta-lactamase in complex with (1R)-1-(2-Thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)-phenyl) methylboronic acid''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2RCX is a [ | + | 2RCX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RCX OCA]. |
==Reference== | ==Reference== | ||
| - | Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors., Morandi S, Morandi F, Caselli E, Shoichet BK, Prati F, Bioorg Med Chem. 2007 Nov 6;. PMID:[http:// | + | Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors., Morandi S, Morandi F, Caselli E, Shoichet BK, Prati F, Bioorg Med Chem. 2007 Nov 6;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17997318 17997318] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:34:49 2008'' |
Revision as of 16:34, 20 March 2008
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| , resolution 2.000Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ampC, ampA (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AmpC Beta-lactamase in complex with (1R)-1-(2-Thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)-phenyl) methylboronic acid
Overview
Boronic acids have proved to be promising selective inhibitors of beta-lactamases, acting as transition state analogues. Starting from a previously described nanomolar inhibitor of AmpC beta-lactamase, three new inhibitors were designed to gain interactions with highly conserved residues, such as Asn343, and to bind more tightly to the enzyme. Among these, one was obtained by stereoselective synthesis and succeeded in placing its anionic group into the carboxylate binding site of the enzyme, as revealed by X-ray crystallography of the complex inhibitor/AmpC. Nevertheless, it failed at improving affinity, when compared to the lead from which it was derived. The origins of this structural and energetic discrepancy are discussed.
About this Structure
2RCX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure-based optimization of cephalothin-analogue boronic acids as beta-lactamase inhibitors., Morandi S, Morandi F, Caselli E, Shoichet BK, Prati F, Bioorg Med Chem. 2007 Nov 6;. PMID:17997318
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