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3e2f
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3e2f.jpg|left|200px]] | ||
| - | + | ==Crystal structure of mouse kynurenine aminotransferase III, PLP-bound form== | |
| - | + | <StructureSection load='3e2f' size='340' side='right'caption='[[3e2f]], [[Resolution|resolution]] 2.59Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3e2f]] 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=3E2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2F 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]] 2.59Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=3e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2f OCA], [https://pdbe.org/3e2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2f RCSB], [https://www.ebi.ac.uk/pdbsum/3e2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2f 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/e2/3e2f_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=3e2f ConSurf]. | |
| - | + | <div style="clear:both"></div> | |
| - | == | + | == References == |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Cai | + | [[Category: Cai T]] |
| - | [[Category: Han | + | [[Category: Han Q]] |
| - | [[Category: Li | + | [[Category: Li J]] |
| - | [[Category: Robinson | + | [[Category: Robinson R]] |
| - | [[Category: Tagle | + | [[Category: Tagle DA]] |
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Current revision
Crystal structure of mouse kynurenine aminotransferase III, PLP-bound form
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Categories: Large Structures | Mus musculus | Cai T | Han Q | Li J | Robinson R | Tagle DA

