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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 1.15&Aring;" />
'''Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase'''<br />


==About this Structure==
==Crystal Structure of T.th.HB8 Serine Hydroxymethyltransferase==
2DKJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DKJ OCA].
<StructureSection load='2dkj' size='340' side='right'caption='[[2dkj]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
[[Category: Glycine hydroxymethyltransferase]]
== Structural highlights ==
[[Category: Single protein]]
<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>
[[Category: Thermus thermophilus]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
[[Category: Goto, M.]]
<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>
[[Category: Hirotsu, K.]]
<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>
[[Category: Kai, K.]]
</table>
[[Category: Miyahara, I.]]
== Function ==
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[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]
[[Category: PLP]]
== Evolutionary Conservation ==
[[Category: SO4]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: national project on protein structural and functional analyses]]
Check<jmol>
[[Category: nppsfa]]
  <jmolCheckbox>
[[Category: plp dependent enzyme]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/2dkj_consurf.spt"</scriptWhenChecked>
[[Category: riken structural genomics/proteomics initiative]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: rsgi]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: structural genomics]]
  </jmolCheckbox>
[[Category: transferase]]
</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>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:55:26 2008''
==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]]

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

2dkj is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2dkj, resolution 1.15Å

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