3pgy
From Proteopedia
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| - | {{STRUCTURE_3pgy| PDB=3pgy | SCENE= }} | ||
| - | ===Serine hydroxymethyltransferase from Staphylococcus aureus, S95P mutant.=== | ||
| - | == | + | ==Serine hydroxymethyltransferase from Staphylococcus aureus, S95P mutant.== |
| - | [[http://www.uniprot.org/uniprot/GLYA_STAAC GLYA_STAAC | + | <StructureSection load='3pgy' size='340' side='right'caption='[[3pgy]], [[Resolution|resolution]] 1.92Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3pgy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGY 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]] 1.92Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</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=3pgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgy OCA], [https://pdbe.org/3pgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pgy RCSB], [https://www.ebi.ac.uk/pdbsum/3pgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pgy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLYA_STAAC GLYA_STAAC] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity).[HAMAP-Rule:MF_00051] | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Staphylococcus aureus]] | + | </StructureSection> |
| - | [[Category: Anderson | + | [[Category: Large Structures]] |
| - | + | [[Category: Staphylococcus aureus subsp. aureus COL]] | |
| - | [[Category: Joachimiak | + | [[Category: Anderson WF]] |
| - | [[Category: Kwon | + | [[Category: Joachimiak A]] |
| - | [[Category: Makowska-Grzyska | + | [[Category: Kwon K]] |
| - | [[Category: Osipiuk | + | [[Category: Makowska-Grzyska M]] |
| - | + | [[Category: Osipiuk J]] | |
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Current revision
Serine hydroxymethyltransferase from Staphylococcus aureus, S95P mutant.
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