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4rx3
From Proteopedia
(Difference between revisions)
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<StructureSection load='4rx3' size='340' side='right' caption='[[4rx3]], [[Resolution|resolution]] 1.39Å' scene=''> | <StructureSection load='4rx3' size='340' side='right' caption='[[4rx3]], [[Resolution|resolution]] 1.39Å' scene=''> | ||
== Structural highlights == | == 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 [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=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> |
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rva|4rva]], [[4rx2|4rx2]]</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='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=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> | <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> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4rx3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4rx3" style="background-color:#fffaf0;"></div> | ||
| - | |||
| - | ==See Also== | ||
| - | *[[Beta-lactamase|Beta-lactamase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Chow, D]] | [[Category: Chow, D]] | ||
Revision as of 09:11, 22 November 2017
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
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