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[[Image:2oql.jpg|left|200px]]


{{Structure
==Structure of Phosphotriesterase mutant H254Q/H257F==
|PDB= 2oql |SIZE=350|CAPTION= <scene name='initialview01'>2oql</scene>, resolution 1.800&Aring;
<StructureSection load='2oql' size='340' side='right'caption='[[2oql]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+401'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+A+402'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B+401'>AC3</scene>, <scene name='pdbsite=AC4:Zn+Binding+Site+For+Residue+B+402'>AC4</scene>, <scene name='pdbsite=AC5:Btb+Binding+Site+For+Residue+A+701'>AC5</scene>, <scene name='pdbsite=AC6:Btb+Binding+Site+For+Residue+B+701'>AC6</scene>, <scene name='pdbsite=AC7:Gol+Binding+Site+For+Residue+B+801'>AC7</scene>, <scene name='pdbsite=AC8:Gol+Binding+Site+For+Residue+A+802'>AC8</scene> and <scene name='pdbsite=AC9:Gol+Binding+Site+For+Residue+B+803'>AC9</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
<table><tr><td colspan='2'>[[2oql]] is a 2 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=2OQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OQL FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1]  
</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>
|GENE= opd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=293 Brevundimonas diminuta])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</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=2oql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oql OCA], [https://pdbe.org/2oql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oql RCSB], [https://www.ebi.ac.uk/pdbsum/2oql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oql 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/oq/2oql_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=2oql ConSurf].
<div style="clear:both"></div>


'''Structure of Phosphotriesterase mutant H254Q/H257F'''
==See Also==
 
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
2OQL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQL OCA].
[[Category: Aryldialkylphosphatase]]
[[Category: Brevundimonas diminuta]]
[[Category: Brevundimonas diminuta]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Almo, S C.]]
[[Category: Almo SC]]
[[Category: Kim, J.]]
[[Category: Kim J]]
[[Category: Raushel, F M.]]
[[Category: Raushel FM]]
[[Category: Tsai, P.]]
[[Category: Tsai P]]
[[Category: BTB]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: hydrolase]]
[[Category: metalloenzyme]]
[[Category: nerve agent]]
[[Category: tim barrel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:03:12 2008''

Latest revision as of 03:22, 28 December 2023

Structure of Phosphotriesterase mutant H254Q/H257FStructure of Phosphotriesterase mutant H254Q/H257F

Structural highlights

2oql is a 2 chain structure with sequence from Brevundimonas diminuta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2oql, resolution 1.80Å

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