View source for 3urq


==Crystal Structure of PTE mutant H254G/H257W/L303T/M317L/I106C/F132I/L271I/K185R/I274N/A80V/R67H with cyclohexyl methylphosphonate inhibitor==
<StructureSection load='3urq' size='340' side='right'caption='[[3urq]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3urq]] 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=3URQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3URQ 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=QMP:CYCLOHEXYL+METHYLPHOSPHONATE'>QMP</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=3urq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3urq OCA], [https://pdbe.org/3urq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3urq RCSB], [https://www.ebi.ac.uk/pdbsum/3urq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3urq 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.

==See Also==
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
__TOC__
</StructureSection>
[[Category: Brevundimonas diminuta]]
[[Category: Large Structures]]
[[Category: Barondeau DP]]
[[Category: Fox NG]]
[[Category: Li Y]]
[[Category: Raushel FM]]
[[Category: Tsai P]]