1ykc: Difference between revisions

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==human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide==
==human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide==
<StructureSection load='1ykc' size='340' side='right' caption='[[1ykc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1ykc' size='340' side='right'caption='[[1ykc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ykc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YKC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ykc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YKC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YKC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDS:OXIDIZED+GLUTATHIONE+DISULFIDE'>GDS</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gtu|2gtu]], [[1xw5|1xw5]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gtu|2gtu]], [[1xw5|1xw5]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTM2, GST4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTM2, GST4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ykc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ykc OCA], [http://pdbe.org/1ykc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ykc RCSB], [http://www.ebi.ac.uk/pdbsum/1ykc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ykc ProSAT]</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=1ykc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ykc OCA], [http://pdbe.org/1ykc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ykc RCSB], [http://www.ebi.ac.uk/pdbsum/1ykc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ykc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yk/1ykc_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yk/1ykc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</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=1ykc ConSurf].
</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=1ykc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Almo, S C]]
[[Category: Listowsky, I]]
[[Category: Listowsky, I]]

Revision as of 11:47, 20 January 2021

human glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfidehuman glutathione S-transferase m2-2 (E.C.2.5.1.18) complexed with glutathione-disulfide

Structural highlights

1ykc is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:GSTM2, GST4 (HUMAN)
Activity:Glutathione transferase, with EC number 2.5.1.18
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[GSTM2_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.[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. Norrgard MA, Ivarsson Y, Tars K, Mannervik B. Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution. Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):4876-81. Epub 2006 Mar 20. PMID:16549767

1ykc, resolution 2.10Å

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