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[[Image:1xm8.jpg|left|200px]]<br /><applet load="1xm8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xm8, resolution 1.74&Aring;" />
'''X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350'''<br />


==About this Structure==
==X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350==
1XM8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=ACY:'>ACY</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XM8 OCA].  
<StructureSection load='1xm8' size='340' side='right'caption='[[1xm8]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</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>
 
==See Also==
*[[Glyoxalase 3D structures|Glyoxalase 3D structures]]
== References ==
<references/>
__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: ACY]]
[[Category: FE]]
[[Category: PEG]]
[[Category: ZN]]
[[Category: at2g31350]]
[[Category: b-lactamase fold]]
[[Category: center for eukaryotic structural genomics]]
[[Category: cesg]]
[[Category: metallo-hydrolase]]
[[Category: mitochondrial isozyme]]
[[Category: protein structure initiative]]
[[Category: psi]]
[[Category: structural genomics]]
[[Category: thioester hydrolase]]
[[Category: zinc/iron binuclear center]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:16:29 2008''

Latest revision as of 11:51, 14 February 2024

X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350X-RAY STRUCTURE OF GLYOXALASE II FROM ARABIDOPSIS THALIANA GENE AT2G31350

Structural highlights

1xm8 is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.74Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

GLO2N_ARATH Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Marasinghe GP, Sander IM, Bennett B, Periyannan G, Yang KW, Makaroff CA, Crowder MW. Structural studies on a mitochondrial glyoxalase II. J Biol Chem. 2005 Dec 9;280(49):40668-75. Epub 2005 Oct 14. PMID:16227621 doi:10.1074/jbc.M509748200

1xm8, resolution 1.74Å

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