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4gy1
From Proteopedia
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<StructureSection load='4gy1' size='340' side='right'caption='[[4gy1]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='4gy1' size='340' side='right'caption='[[4gy1]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4gy1]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4gy1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GY1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</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=4gy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gy1 OCA], [https://pdbe.org/4gy1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gy1 RCSB], [https://www.ebi.ac.uk/pdbsum/4gy1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gy1 ProSAT]</span></td></tr> | |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
| - | *[[Phosphotriesterase|Phosphotriesterase]] | + | *[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Synthetic construct | + | [[Category: Synthetic construct]] |
| - | [[Category: Jackson | + | [[Category: Jackson CJ]] |
| - | [[Category: Tawfik | + | [[Category: Tawfik DS]] |
| - | [[Category: Tokuriki | + | [[Category: Tokuriki N]] |
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Revision as of 07:25, 26 October 2022
Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate
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