8p7n: Difference between revisions
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New page: '''Unreleased structure''' The entry 8p7n is ON HOLD Authors: Dym, O., Aggawal, N., Ashani, Y., Albeck, S., Unger, T., Hamer Rogotner, S., Silman, I., Sussman, J.L. Description: The im... |
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The entry 8p7n is | ==The impact of molecular variants, crystallization conditions and space group on structure-ligand complexes: A case study on Bacterial Phosphotriesterase Variants and complexes== | ||
<StructureSection load='8p7n' size='340' side='right'caption='[[8p7n]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8p7n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6fu0 6fu0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P7N 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]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=8p7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p7n OCA], [https://pdbe.org/8p7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p7n RCSB], [https://www.ebi.ac.uk/pdbsum/8p7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p7n 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__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Brevundimonas diminuta]] | ||
[[Category: Albeck | [[Category: Large Structures]] | ||
[[Category: | [[Category: Aggarwal N]] | ||
[[Category: | [[Category: Albeck S]] | ||
[[Category: | [[Category: Ashani Y]] | ||
[[Category: | [[Category: Dym O]] | ||
[[Category: | [[Category: Hamer Rogotner S]] | ||
[[Category: | [[Category: Silman I]] | ||
[[Category: Sussman JL]] | |||
[[Category: Unger T]] | |||
Latest revision as of 20:03, 8 November 2023
The impact of molecular variants, crystallization conditions and space group on structure-ligand complexes: A case study on Bacterial Phosphotriesterase Variants and complexesThe impact of molecular variants, crystallization conditions and space group on structure-ligand complexes: A case study on Bacterial Phosphotriesterase Variants and complexes
Structural highlights
FunctionOPD_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 |
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