2xr0
From Proteopedia
(Difference between revisions)
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<StructureSection load='2xr0' size='340' side='right'caption='[[2xr0]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2xr0' size='340' side='right'caption='[[2xr0]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2xr0]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xr0]] is a 1 chain structure with sequence from [https://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=2XR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XR0 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iyp|1iyp]], [[1we4|1we4]], [[2wyx|2wyx]], [[1iys|1iys]], [[1iyo|1iyo]], [[1bza|1bza]], [[1iyq|1iyq]], [[2xqz|2xqz]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1iyp|1iyp]], [[1we4|1we4]], [[2wyx|2wyx]], [[1iys|1iys]], [[1iyo|1iyo]], [[1bza|1bza]], [[1iyq|1iyq]], [[2xqz|2xqz]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xr0 OCA], [https://pdbe.org/2xr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2xr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xr0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX]] Has strong cefotaxime-hydrolyzing activity. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 12:15, 27 April 2022
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
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