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3e2y

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Current revision (12:57, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3e2y' size='340' side='right'caption='[[3e2y]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
<StructureSection load='3e2y' size='340' side='right'caption='[[3e2y]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3e2y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e2f|3e2f]], [[3e2z|3e2z]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ccbl2, Kat3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
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<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>
<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>
</table>
== Function ==
== Function ==
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[[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>
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Mus musculus]]
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[[Category: Cai, T]]
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[[Category: Cai T]]
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[[Category: Han, Q]]
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[[Category: Han Q]]
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[[Category: Li, J]]
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[[Category: Li J]]
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[[Category: Robinson, R]]
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[[Category: Robinson R]]
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[[Category: Tagle, D A]]
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[[Category: Tagle DA]]
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[[Category: Alpha beta protein]]
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[[Category: Aminotransferase]]
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[[Category: Lyase]]
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[[Category: Plp dependent protein]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Transferase]]
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Current revision

Crystal structure of mouse kynurenine aminotransferase III in complex with glutamine

PDB ID 3e2y

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