3ecd

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Current revision (13:00, 30 August 2023) (edit) (undo)
 
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<StructureSection load='3ecd' size='340' side='right'caption='[[3ecd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3ecd' size='340' side='right'caption='[[3ecd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ecd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ECD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ECD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ecd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ECD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ECD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glyA2, BPSS0547 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ecd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ecd OCA], [https://pdbe.org/3ecd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ecd RCSB], [https://www.ebi.ac.uk/pdbsum/3ecd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ecd ProSAT]</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=3ecd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ecd OCA], [https://pdbe.org/3ecd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ecd RCSB], [https://www.ebi.ac.uk/pdbsum/3ecd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ecd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLYA2_BURPS GLYA2_BURPS]] 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]
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[https://www.uniprot.org/uniprot/GLYA2_BURP1 GLYA2_BURP1] 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]]
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==See Also==
==See Also==
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*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]]
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*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus pseudomallei whitmore 1913]]
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[[Category: Burkholderia pseudomallei]]
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[[Category: Glycine hydroxymethyltransferase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
 
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[[Category: Bupsa00008a]]
 
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[[Category: Decode]]
 
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[[Category: One-carbon metabolism]]
 
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[[Category: Pyridoxal phosphate]]
 
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[[Category: Ssgcid]]
 
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[[Category: Transferase]]
 

Current revision

Crystal structure of serine hydroxymethyltransferase from Burkholderia pseudomallei

PDB ID 3ecd

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