2dkj
From Proteopedia
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| - | [[Image:2dkj.gif|left|200px]]<br /><applet load="2dkj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2dkj, resolution 1.15Å" /> | ||
| - | '''Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase'''<br /> | ||
| - | == | + | ==Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase== |
| - | + | <StructureSection load='2dkj' size='340' side='right'caption='[[2dkj]], [[Resolution|resolution]] 1.15Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2dkj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DKJ 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]] 1.15Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2dkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dkj OCA], [https://pdbe.org/2dkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dkj RCSB], [https://www.ebi.ac.uk/pdbsum/2dkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dkj ProSAT], [https://www.topsan.org/Proteins/RSGI/2dkj TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/GLYA_THET8 GLYA_THET8] 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.[HAMAP-Rule:MF_00051] | |
| - | [ | + | == 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/dk/2dkj_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=2dkj ConSurf]. | |
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus HB8]] | ||
| + | [[Category: Goto M]] | ||
| + | [[Category: Hirotsu K]] | ||
| + | [[Category: Kai K]] | ||
| + | [[Category: Miyahara I]] | ||
Current revision
Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase
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