1xpb
From Proteopedia
(New page: 200px<br /> <applet load="1xpb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xpb, resolution 1.90Å" /> '''STRUCTURE OF BETA-L...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1XPB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1XPB OCA]]. | + | 1XPB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with SO4 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]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XPB OCA]]. |
==Reference== | ==Reference== | ||
TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant., Fonze E, Charlier P, To'th Y, Vermeire M, Raquet X, Dubus A, Frere JM, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):682-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299797 15299797] | TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant., Fonze E, Charlier P, To'th Y, Vermeire M, Raquet X, Dubus A, Frere JM, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):682-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299797 15299797] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transposable element]] | [[Category: transposable element]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:31:48 2007'' |
Revision as of 10:27, 30 October 2007
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STRUCTURE OF BETA-LACTAMASE TEM1
Overview
beta-Lactamases are bacterial enzymes which catalyse the hydrolysis of the, beta-lactam ring of penicillins, cephalosporins and related compounds, thus inactivating these antibiotics. The crystal structure of the TEM1, beta-lactamase has been determined at 1.9 A resolution by the, molecular-replacement method, using the atomic coordinates of two, homologous beta-lactamase refined structures which show about 36% strict, identity in their amino-acid sequences and 1.96 A r.m.s. deviation between, equivalent Calpha atoms. The TEM1 enzyme crystallizes in space group, P2(1)2(1)2(1) and there is one molecule per asymmetric unit. The structure, was refined by simulated annealing to an R-factor of 15.6% for 15 086, reflections with I >/= 2sigma(I) in the resolution range 5.0-1.9 A. The, final ... [(full description)]
About this Structure
1XPB is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant., Fonze E, Charlier P, To'th Y, Vermeire M, Raquet X, Dubus A, Frere JM, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):682-94. PMID:15299797
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