6ayk
From Proteopedia
(Difference between revisions)
m (Protected "6ayk" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of TEM1 beta-lactamase mutant I263A in the presence of 1.2 MPa xenon== | |
| - | + | <StructureSection load='6ayk' size='340' side='right' caption='[[6ayk]], [[Resolution|resolution]] 1.44Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ayk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AYK FirstGlance]. <br> | |
| - | + | </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: | + | <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=6ayk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ayk OCA], [http://pdbe.org/6ayk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ayk RCSB], [http://www.ebi.ac.uk/pdbsum/6ayk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ayk 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: Beta-lactamase]] | ||
| + | [[Category: Dmochowski, I J]] | ||
| + | [[Category: Roose, B W]] | ||
| + | [[Category: Enzyme]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Xenon]] | ||
Revision as of 07:33, 12 September 2018
Crystal structure of TEM1 beta-lactamase mutant I263A in the presence of 1.2 MPa xenon
| |||||||||||
