1y54

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(New page: 200px<br /><applet load="1y54" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y54, resolution 2.10&Aring;" /> '''Crystal structure of...)
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[[Image:1y54.gif|left|200px]]<br /><applet load="1y54" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1y54.gif|left|200px]]<br /><applet load="1y54" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1y54, resolution 2.10&Aring;" />
caption="1y54, resolution 2.10&Aring;" />
'''Crystal structure of the native class C beta-lactamase from Enterobacter cloacae 908R complexed with BRL42715'''<br />
'''Crystal structure of the native class C beta-lactamase from Enterobacter cloacae 908R complexed with BRL42715'''<br />
==Overview==
==Overview==
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BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial -lactamases. The crystal structure of Enterobacter cloacae 908R class C -lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C -lactamase.
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BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial beta-lactamases. The crystal structure of Enterobacter cloacae 908R class C beta-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C beta-lactamase.
==About this Structure==
==About this Structure==
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1Y54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with FDT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y54 OCA].
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1Y54 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae] with <scene name='pdbligand=FDT:'>FDT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y54 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Charlier, P.]]
[[Category: Charlier, P.]]
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[[Category: Frere, J.M.]]
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[[Category: Frere, J M.]]
[[Category: Michaux, C.]]
[[Category: Michaux, C.]]
[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
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[[Category: class c beta-lactamase]]
[[Category: class c beta-lactamase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:34:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:51 2008''

Revision as of 14:01, 21 February 2008


1y54, resolution 2.10Å

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Crystal structure of the native class C beta-lactamase from Enterobacter cloacae 908R complexed with BRL42715

Overview

BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, is an active-site-directed inactivator of bacterial beta-lactamases. The crystal structure of Enterobacter cloacae 908R class C beta-lactamase in complex with BRL 42715, docking, and energy minimization studies explain stereoselectivity of the binding of C6-(heterocyclic methylene)penems against class C beta-lactamase.

About this Structure

1Y54 is a Single protein structure of sequence from Enterobacter cloacae with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Crystal structure of BRL 42715, C6-(N1-methyl-1,2,3-triazolylmethylene)penem, in complex with Enterobacter cloacae 908R beta-lactamase: evidence for a stereoselective mechanism from docking studies., Michaux C, Charlier P, Frere JM, Wouters J, J Am Chem Soc. 2005 Mar 16;127(10):3262-3. PMID:15755127

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