5eht: Difference between revisions

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<StructureSection load='5eht' size='340' side='right'caption='[[5eht]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
<StructureSection load='5eht' size='340' side='right'caption='[[5eht]], [[Resolution|resolution]] 1.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5eht]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EHT FirstGlance]. <br>
<table><tr><td colspan='2'>[[5eht]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EHT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.29&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eh9|5eh9]]</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=5eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eht OCA], [https://pdbe.org/5eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eht RCSB], [https://www.ebi.ac.uk/pdbsum/5eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eht ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aiiA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1428 "Bacillus cereus var. thuringiensis" Smith et al. 1952])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quorum-quenching_N-acyl-homoserine_lactonase Quorum-quenching N-acyl-homoserine lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.81 3.1.1.81] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eht OCA], [http://pdbe.org/5eht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eht RCSB], [http://www.ebi.ac.uk/pdbsum/5eht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eht ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/AHLL_BACTU AHLL_BACTU]] Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.<ref>PMID:15895999</ref>
[https://www.uniprot.org/uniprot/AHLL_BACTU AHLL_BACTU] Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.<ref>PMID:15895999</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus cereus var. thuringiensis smith et al. 1952]]
[[Category: Bacillus thuringiensis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Quorum-quenching N-acyl-homoserine lactonase]]
[[Category: Hong N-S]]
[[Category: Hong, N S]]
[[Category: Jackson CJ]]
[[Category: Jackson, C J]]
[[Category: Aiia]]
[[Category: Directed evolution]]
[[Category: Hydrolase]]
[[Category: Lactonase]]
[[Category: N-acyl-homoserine lactonase]]
[[Category: Paraoxonase]]
[[Category: Phosphatase]]
[[Category: Qql]]
Retrieved from "https://proteopedia.org/5eht"