4qy5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations==
==Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations==
-
<StructureSection load='4qy5' size='340' side='right' caption='[[4qy5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+
<StructureSection load='4qy5' size='340' side='right'caption='[[4qy5]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4qy5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QY5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4qy5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QY5 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>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qy5 OCA], [https://pdbe.org/4qy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qy5 RCSB], [https://www.ebi.ac.uk/pdbsum/4qy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qy5 ProSAT]</span></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, pse4, carB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=4qy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qy5 OCA], [http://pdbe.org/4qy5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qy5 RCSB], [http://www.ebi.ac.uk/pdbsum/4qy5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qy5 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== 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.
+
[https://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.[https://www.uniprot.org/uniprot/BLP4_PSEAI BLP4_PSEAI] Hydrolyzes both carbenicillin and oxacillin.
 +
 
 +
==See Also==
 +
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Beta-lactamase]]
+
[[Category: Escherichia coli]]
-
[[Category: Berghuis, A M]]
+
[[Category: Large Structures]]
-
[[Category: Gobeil, S]]
+
[[Category: Pseudomonas aeruginosa]]
-
[[Category: Park, J]]
+
[[Category: Berghuis AM]]
-
[[Category: Pelletier, J N]]
+
[[Category: Gobeil S]]
-
[[Category: Hydrolase]]
+
[[Category: Park J]]
 +
[[Category: Pelletier JN]]

Revision as of 13:58, 22 February 2023

Crystal structures of chimeric beta-lactamase cTEM-19m showing different conformations

PDB ID 4qy5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qy5"
Personal tools