5i63: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5i63 is ~~ON HOLD until Paper Publication~~

==Crystal structure of TEM1 beta-lactamase mutant I263N in the presence of 1.2 MPa xenon==

~~Authors~~:

== Structural highlights ==

<table><tr><td colspan='2'>[[5i63]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I63 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I63 FirstGlance].

~~Description~~:

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=XE:XENON'>XE</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5i52|5i52]]</td></tr>

<tr id='gene'><td class="sblockLbl">[[Gene|Gene:]]</td><td class="sblockDat">bla, blaT-3, blaT-4, blaT-5, blaT-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i63 OCA], [http://pdbe.org/5i63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i63 RCSB], [http://www.ebi.ac.uk/pdbsum/5i63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i63 ProSAT]</td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.

__TOC__

</StructureSection>

[[Category: Bacillus coli migula 1895]]

[[Category: Beta-lactamase]]

[[Category: Dmochowski, I J]]

[[Category: Roose, B W]]

[[Category: Hydrolase]]

[[Category: Xenon]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5i63 is ON HOLD  until Paper Publication
+==Crystal structure of TEM1 beta-lactamase mutant I263N in the presence of 1.2 MPa xenon==
+<StructureSection load='5i63' size='340' side='right' caption='[[5i63]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5i63]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I63 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I63 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i52|5i52]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bla, blaT-3, blaT-4, blaT-5, blaT-6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i63 OCA], [http://pdbe.org/5i63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i63 RCSB], [http://www.ebi.ac.uk/pdbsum/5i63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i63 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/BLAT_ECOLX BLAT_ECOLX]] TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
+__TOC__
+</StructureSection>
+[[Category: Bacillus coli migula 1895]]
+[[Category: Beta-lactamase]]
+[[Category: Dmochowski, I J]]
+[[Category: Roose, B W]]
+[[Category: Hydrolase]]
+[[Category: Xenon]]