1flj: Difference between revisions

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 <StructureSection load='1flj' size='340' side='right'caption='[[1flj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1flj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FLJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1flj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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]] 1.8&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </span></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=1flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flj OCA], [https://pdbe.org/1flj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1flj RCSB], [https://www.ebi.ac.uk/pdbsum/1flj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flj ProSAT]</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=1flj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flj OCA], [http://pdbe.org/1flj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1flj RCSB], [http://www.ebi.ac.uk/pdbsum/1flj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1flj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAH3_RAT CAH3_RAT]] Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.
+[https://www.uniprot.org/uniprot/CAH3_RAT CAH3_RAT] Reversible hydration of carbon dioxide. A major participant in the liver response to oxidative stress.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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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=1flj ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-S-Glutathiolation of carbonic anhydrase III (CAIII) occurs rapidly in hepatocytes under oxidative stress. The crystal structure of the S-glutathiolated CAIII from rat liver reveals covalent adducts on cysteines 183 and 188. Electrostatic charge and steric contacts at each modification site inversely correlate with the relative rates of reactivity of these cysteines toward glutathione (GSH). Diffuse electron density associated with the GSH adducts suggests a lack of preferred bonding interactions between CAIII and the glutathionyl moieties. Hence, the GSH adducts are available for binding by a protein capable of reducing this mixed disulfide. These properties are consistent with the participation of CAIII in the protection/recovery from the damaging effects of oxidative agents.
-Crystal structure of S-glutathiolated carbonic anhydrase III.,Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA FEBS Lett. 2000 Oct 6;482(3):237-41. PMID:11024467<ref>PMID:11024467</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1flj" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Carbonate dehydratase]]
 [[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Chatterjee, T K]]
+[[Category: Chatterjee TK]]
-[[Category: Darmawan, S]]
+[[Category: Darmawan S]]
-[[Category: Fisher, R A]]
+[[Category: Fisher RA]]
-[[Category: Honzatko, R B]]
+[[Category: Honzatko RB]]
-[[Category: Mallis, R J]]
+[[Category: Mallis RJ]]
-[[Category: Poland, B W]]
+[[Category: Poland BW]]
-[[Category: Thomas, J A]]
+[[Category: Thomas JA]]
-[[Category: Carbonic anhydrase iii]]
-[[Category: Glutathione]]
-[[Category: Lyase]]
-[[Category: S-glutathiolated]]
-[[Category: S-glutathionylated]]