5gst

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:11, 30 August 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:5gst.gif|left|200px]]
 
-
{{Structure
+
==REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE==
-
|PDB= 5gst |SIZE=350|CAPTION= <scene name='initialview01'>5gst</scene>, resolution 2.0&Aring;
+
<StructureSection load='5gst' size='340' side='right'caption='[[5gst]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=GDN:GLUTATHIONE+S-(2,4+DINITROBENZENE)'>GDN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
<table><tr><td colspan='2'>[[5gst]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GST FirstGlance]. <br>
-
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDN:GLUTATHIONE+S-(2,4+DINITROBENZENE)'>GDN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gst OCA], [https://pdbe.org/5gst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gst RCSB], [https://www.ebi.ac.uk/pdbsum/5gst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gst ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gst OCA], [http://www.ebi.ac.uk/pdbsum/5gst PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5gst RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/GSTM1_RAT GSTM1_RAT] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The olfactory GST may be crucial for the acuity of the olfactory process.
 +
== 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/gs/5gst_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=5gst ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.
-
'''REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE'''
+
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase.,Ji X, Armstrong RN, Gilliland GL Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:8241147<ref>PMID:8241147</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 5gst" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The three-dimensional structures of a class mu glutathione transferase in complex with a transition-state analogue, 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate, and a product, 1-(S-glutathionyl)-2,4-dinitrobenzene, of a nucleophilic aromatic substitution (SNAr) reaction have been determined at 1.9- and 2.0-A resolution, respectively. The two structures represent snapshots along the reaction coordinate for the enzyme-catalyzed reaction of glutathione with 1-chloro-2,4-dinitrobenzene and reveal specific interactions between the enzyme, intermediate, and product that are important in catalysis. The geometries of the intermediate and product are used to postulate reaction coordinate motion during catalysis.
+
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
5GST is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GST OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase., Ji X, Armstrong RN, Gilliland GL, Biochemistry. 1993 Dec 7;32(48):12949-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8241147 8241147]
+
-
[[Category: Glutathione transferase]]
+
[[Category: Rattus rattus]]
[[Category: Rattus rattus]]
-
[[Category: Single protein]]
+
[[Category: Armstrong RN]]
-
[[Category: Armstrong, R N.]]
+
[[Category: Gilliland GL]]
-
[[Category: Gilliland, G L.]]
+
[[Category: Ji X]]
-
[[Category: Ji, X.]]
+
-
[[Category: glutathione transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:41:32 2008''
+

Current revision

REACTION COORDINATE MOTION IN AN SNAR REACTION CATALYZED BY GLUTATHIONE TRANSFERASE

PDB ID 5gst

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5gst"
Personal tools