8bv4: Difference between revisions
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==Structure of BlaC from Mycobacterium tuberculosis in complex with vaborbactam== | |||
<StructureSection load='8bv4' size='340' side='right'caption='[[8bv4]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8bv4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BV4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4D6:{(3R,6S)-2-HYDROXY-3-[(THIOPHEN-2-YLACETYL)AMINO]-1,2-OXABORINAN-6-YL}ACETIC+ACID'>4D6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bv4 OCA], [https://pdbe.org/8bv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bv4 RCSB], [https://www.ebi.ac.uk/pdbsum/8bv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bv4 ProSAT]</span></td></tr> | ||
[[Category: Bruenle | </table> | ||
[[Category: Ubbink | == Function == | ||
[https://www.uniprot.org/uniprot/BLAC_MYCTA BLAC_MYCTA] Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics.[UniProtKB:P9WKD3]<ref>PMID:9624479</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Bruenle S]] | |||
[[Category: Chikunova A]] | |||
[[Category: Ubbink M]] | |||
Latest revision as of 11:19, 7 February 2024
Structure of BlaC from Mycobacterium tuberculosis in complex with vaborbactamStructure of BlaC from Mycobacterium tuberculosis in complex with vaborbactam
Structural highlights
FunctionBLAC_MYCTA Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics.[UniProtKB:P9WKD3][1] References
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