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| - | | + | #REDIRECT [[8p7k]] This PDB entry is obsolete and replaced by 8p7k |
| - | ==Phosphotriesterase PTE_A53_4==
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| - | <StructureSection load='6fev' size='340' side='right' caption='[[6fev]], [[Resolution|resolution]] 1.93Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[6fev]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FEV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FEV FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=E5N:(2~{R})-2-methylpentanedioic+acid'>E5N</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6fee|6fee]], [[6fef|6fef]], [[6fei|6fei]]</td></tr>
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| - | <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>
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| - | <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=6fev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fev OCA], [http://pdbe.org/6fev PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fev RCSB], [http://www.ebi.ac.uk/pdbsum/6fev PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fev ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[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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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Aryldialkylphosphatase]]
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| - | [[Category: Aggarwal, N]]
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| - | [[Category: Albeck, S]]
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| - | [[Category: Ashani, Y]]
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| - | [[Category: Dym, O]]
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| - | [[Category: Goldsmith, M]]
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| - | [[Category: Greisen, P]]
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| - | [[Category: Leader, H]]
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| - | [[Category: Rogotner, S Hamer]]
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| - | [[Category: Silman, I]]
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| - | [[Category: Sussman, L J]]
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| - | [[Category: Tawfik, D]]
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| - | [[Category: Unger, T]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Metalloenzyme]]
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| - | [[Category: Tim barrel]]
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