View source for 6fqe


==Phosphotriesterase PTE_A53_4==
<StructureSection load='6fqe' size='340' side='right'caption='[[6fqe]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fqe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FQE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D6K:(4~{S},6~{R})-2,2,6-trimethyl-1,3-dioxan-4-ol'>D6K</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=6fqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fqe OCA], [http://pdbe.org/6fqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fqe RCSB], [http://www.ebi.ac.uk/pdbsum/6fqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fqe ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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. 
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</StructureSection>
[[Category: Aryldialkylphosphatase]]
[[Category: Large Structures]]
[[Category: Aggarwal, N]]
[[Category: Albeck, S]]
[[Category: Ashani, Y]]
[[Category: Dym, O]]
[[Category: Goldsmith, M]]
[[Category: Greisen, P]]
[[Category: Leader, H]]
[[Category: Rogotner, S Hamer]]
[[Category: Silman, I]]
[[Category: Sussman, L J]]
[[Category: Tawfik, D]]
[[Category: Unger, T]]
[[Category: Hydrolase]]
[[Category: Metalloenzyme]]
[[Category: Tim barrel]]