2o4m: Difference between revisions
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New page: left|200px<br /><applet load="2o4m" size="350" color="white" frame="true" align="right" spinBox="true" caption="2o4m, resolution 1.640Å" /> '''Structure of Phosph... |
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== | ==Structure of Phosphotriesterase mutant I106G/F132G/H257Y== | ||
<StructureSection load='2o4m' size='340' side='right'caption='[[2o4m]], [[Resolution|resolution]] 1.64Å' scene=''> | |||
[[ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2o4m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O4M 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]] 1.64Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2o4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o4m OCA], [https://pdbe.org/2o4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o4m RCSB], [https://www.ebi.ac.uk/pdbsum/2o4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o4m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OPD_BREDI OPD_BREDI] Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o4/2o4m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o4m ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brevundimonas diminuta]] | [[Category: Brevundimonas diminuta]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Almo | [[Category: Almo SC]] | ||
[[Category: Kim | [[Category: Kim J]] | ||
[[Category: Ramagopal | [[Category: Ramagopal UA]] | ||
[[Category: Raushel | [[Category: Raushel FM]] | ||
[[Category: Tsai | [[Category: Tsai P]] | ||
Latest revision as of 13:30, 30 August 2023
Structure of Phosphotriesterase mutant I106G/F132G/H257YStructure of Phosphotriesterase mutant I106G/F132G/H257Y
Structural highlights
FunctionOPD_BREDI Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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