2dkj: Difference between revisions
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<StructureSection load='2dkj' size='340' side='right'caption='[[2dkj]], [[Resolution|resolution]] 1.15Å' scene=''> | <StructureSection load='2dkj' size='340' side='right'caption='[[2dkj]], [[Resolution|resolution]] 1.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dkj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </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=' | <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> | <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> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 22: | ||
==See Also== | ==See Also== | ||
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Goto | [[Category: Goto M]] | ||
[[Category: Hirotsu | [[Category: Hirotsu K]] | ||
[[Category: Kai | [[Category: Kai K]] | ||
[[Category: Miyahara | [[Category: Miyahara I]] | ||
Latest revision as of 11:27, 25 October 2023
Crystal Structure of T.th.HB8 Serine HydroxymethyltransferaseCrystal Structure of T.th.HB8 Serine Hydroxymethyltransferase
Structural highlights
FunctionGLYA_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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