3e2y
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3e2y is ON HOLD Authors: Han, Q., Robinson, R., Cai, T., Tagle, D.A., Li, J. Description: Crystal structure of mouse kynurenine aminotransferase II...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of mouse kynurenine aminotransferase III in complex with glutamine== | |
| - | + | <StructureSection load='3e2y' size='340' side='right'caption='[[3e2y]], [[Resolution|resolution]] 2.26Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3e2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2Y 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]] 2.26Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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=3e2y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2y OCA], [https://pdbe.org/3e2y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2y RCSB], [https://www.ebi.ac.uk/pdbsum/3e2y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2y ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAT3_MOUSE KAT3_MOUSE] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro).<ref>PMID:19029248</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/e2/3e2y_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=3e2y ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Cai T]] | ||
| + | [[Category: Han Q]] | ||
| + | [[Category: Li J]] | ||
| + | [[Category: Robinson R]] | ||
| + | [[Category: Tagle DA]] | ||
Current revision
Crystal structure of mouse kynurenine aminotransferase III in complex with glutamine
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Categories: Large Structures | Mus musculus | Cai T | Han Q | Li J | Robinson R | Tagle DA
