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==DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI==
==DFP-INHIBITED ESTERASE ESTB FROM BURKHOLDERIA GLADIOLI==
<StructureSection load='1ci9' size='340' side='right' caption='[[1ci9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1ci9' size='340' side='right'caption='[[1ci9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ci9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10248 Atcc 10248]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CI9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ci9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_gladioli Burkholderia gladioli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CI9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DFP:DIISOPROPYL+PHOSPHONATE'>DFP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ESTB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28095 ATCC 10248])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DFP:DIISOPROPYL+PHOSPHONATE'>DFP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></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=1ci9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci9 OCA], [https://pdbe.org/1ci9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ci9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ci9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ci9 ProSAT]</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=1ci9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ci9 OCA], [http://pdbe.org/1ci9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ci9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ci9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ci9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ESTB_BURGA ESTB_BURGA]] Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.  
[https://www.uniprot.org/uniprot/ESTB_BURGA ESTB_BURGA] Acts on short-chain (C4-C6) fatty acid esters and triglycerides, including tertiary alcohol esters. Activity on p-nitrophenyl esters is generally higher than on o-nitrophenyl esters. Lacks beta-lactamase activity; it hydrolyzes the ester bond of cephalosporin substrates but there is no opening of the beta-lactam ring observed.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/1ci9_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/1ci9_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 1ci9" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1ci9" style="background-color:#fffaf0;"></div>
==See Also==
*[[Carboxylesterase 3D structures|Carboxylesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 10248]]
[[Category: Burkholderia gladioli]]
[[Category: Carboxylesterase]]
[[Category: Large Structures]]
[[Category: Kratky, C]]
[[Category: Kratky C]]
[[Category: Petersen, E I]]
[[Category: Petersen EI]]
[[Category: Schwab, H]]
[[Category: Schwab H]]
[[Category: Wagner, U G]]
[[Category: Wagner UG]]
[[Category: Caboxylesterase]]
[[Category: Hydrolase]]

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