3kgw
From Proteopedia
(Difference between revisions)
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<StructureSection load='3kgw' size='340' side='right'caption='[[3kgw]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='3kgw' size='340' side='right'caption='[[3kgw]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3kgw]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3kgw]] 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=3KGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KGW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene> | + | </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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=3kgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kgw OCA], [https://pdbe.org/3kgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kgw RCSB], [https://www.ebi.ac.uk/pdbsum/3kgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kgw ProSAT]</span></td></tr> | |
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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 == | == 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]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
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Revision as of 11:43, 1 February 2023
Crystal structure of Putative aminotransferase (AAH25799.1) from MUS MUSCULUS at 1.65 A resolution
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