3kgx
From Proteopedia
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| - | {{STRUCTURE_3kgx| PDB=3kgx | SCENE= }} | ||
| - | ===Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A resolution=== | ||
| - | == | + | ==Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A resolution== |
| - | [[3kgx]] is a 2 chain structure with sequence from [ | + | <StructureSection load='3kgx' size='340' side='right'caption='[[3kgx]], [[Resolution|resolution]] 1.80Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3kgx]] 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=3KGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KGX 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3kgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kgx OCA], [https://pdbe.org/3kgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kgx RCSB], [https://www.ebi.ac.uk/pdbsum/3kgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kgx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AGT1_MOUSE AGT1_MOUSE] Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification.[UniProtKB:P21549] Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-serine metabolism.[UniProtKB:P09139] | ||
| + | == 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/kg/3kgx_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=3kgx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
| - | [[Category: Jcsg]] | ||
| - | [[Category: Joint center for structural genomic]] | ||
| - | [[Category: Protein structure initiative]] | ||
| - | [[Category: Psi-2]] | ||
| - | [[Category: Putative aminotransferase]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Transferase]] | ||
Current revision
Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.80 A resolution
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