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[[Image:1xm8.jpg|left|200px]]


{{Structure
==X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350==
|PDB= 1xm8 |SIZE=350|CAPTION= <scene name='initialview01'>1xm8</scene>, resolution 1.74&Aring;
<StructureSection load='1xm8' size='340' side='right'caption='[[1xm8]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+700'>AC1</scene>, <scene name='pdbsite=AC2:Fe+Binding+Site+For+Residue+A+701'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B+703'>AC3</scene>, <scene name='pdbsite=AC4:Fe+Binding+Site+For+Residue+B+704'>AC4</scene>, <scene name='pdbsite=AC5:Acy+Binding+Site+For+Residue+A+800'>AC5</scene>, <scene name='pdbsite=AC6:Acy+Binding+Site+For+Residue+B+801'>AC6</scene> and <scene name='pdbsite=AC7:Peg+Binding+Site+For+Residue+A+900'>AC7</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[1xm8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XM8 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74&#8491;</td></tr>
|GENE= At2g31350 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK10241 PRK10241]</span>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xm8 OCA], [https://pdbe.org/1xm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xm8 RCSB], [https://www.ebi.ac.uk/pdbsum/1xm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xm8 ProSAT], [https://www.topsan.org/Proteins/CESG/1xm8 TOPSAN]</span></td></tr>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xm8 OCA], [http://www.ebi.ac.uk/pdbsum/1xm8 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1xm8 RCSB]</span>
</table>
}}
== Function ==
[https://www.uniprot.org/uniprot/GLO2N_ARATH GLO2N_ARATH] Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.<ref>PMID:16227621</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xm/1xm8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xm8 ConSurf].
<div style="clear:both"></div>


'''X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350'''
==See Also==
 
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1XM8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XM8 OCA].
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Hydroxyacylglutathione hydrolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Allard STM]]
[[Category: Allard, S T.M.]]
[[Category: Bingman CA]]
[[Category: Bingman, C A.]]
[[Category: Bitto E]]
[[Category: Bitto, E.]]
[[Category: Phillips Jr GN]]
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
[[Category: Smith DW]]
[[Category: Jr., G N.Phillips.]]
[[Category: Wesenberg GE]]
[[Category: Smith, D W.]]
[[Category: Wesenberg, G E.]]
[[Category: at2g31350]]
[[Category: b-lactamase fold]]
[[Category: center for eukaryotic structural genomic]]
[[Category: cesg]]
[[Category: metallo-hydrolase]]
[[Category: mitochondrial isozyme]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomic]]
[[Category: thioester hydrolase]]
[[Category: zinc/iron binuclear center]]
 
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