4qy6
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations== |
| - | + | <StructureSection load='4qy6' size='340' side='right' caption='[[4qy6]], [[Resolution|resolution]] 1.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4qy6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QY6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4id4|4id4]], [[4mez|4mez]]</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=4qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qy6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qy6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qy6 PDBsum]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == 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: Beta-lactamase]] | ||
| + | [[Category: Berghuis, A M]] | ||
[[Category: Gobeil, S]] | [[Category: Gobeil, S]] | ||
| - | [[Category: | + | [[Category: Park, J]] |
| + | [[Category: Pelletier, J N]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 14:45, 12 August 2015
Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations
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