4rx3: Difference between revisions

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 ==A triple mutant in the omega-loop of TEM-1 beta-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis==
-<StructureSection load='4rx3' size='340' side='right' caption='[[4rx3]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
+<StructureSection load='4rx3' size='340' side='right'caption='[[4rx3]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rx3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RX3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rx3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RX3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rva|4rva]], [[4rx2|4rx2]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4rx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx3 OCA], [https://pdbe.org/4rx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rx3 RCSB], [https://www.ebi.ac.uk/pdbsum/4rx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rx3 ProSAT]</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=4rx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rx3 OCA], [http://pdbe.org/4rx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rx3 RCSB], [http://www.ebi.ac.uk/pdbsum/4rx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rx3 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.
+[https://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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 ==See Also==
-*[[Beta-lactamase|Beta-lactamase]]
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Beta-lactamase]]
+[[Category: Escherichia coli]]
-[[Category: Chow, D]]
+[[Category: Large Structures]]
-[[Category: Gilbert, H]]
+[[Category: Chow D]]
-[[Category: Hu, L]]
+[[Category: Gilbert H]]
-[[Category: Palzkill, T]]
+[[Category: Hu L]]
-[[Category: Prasad, B V.V]]
+[[Category: Palzkill T]]
-[[Category: Sankaran, B]]
+[[Category: Prasad BVV]]
-[[Category: Stojanoski, V]]
+[[Category: Sankaran B]]
-[[Category: Globular]]
+[[Category: Stojanoski V]]
-[[Category: Hydrolase]]