4otl: Difference between revisions

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New page: '''Unreleased structure''' The entry 4otl is ON HOLD Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Description: X-ray Crystal Structure of Serine Hydroxym...
 
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'''Unreleased structure'''


The entry 4otl is ON HOLD
==X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Glycine==
<StructureSection load='4otl' size='340' side='right'caption='[[4otl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4otl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OTL 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=4otl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4otl OCA], [https://pdbe.org/4otl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4otl RCSB], [https://www.ebi.ac.uk/pdbsum/4otl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4otl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4ECY9_BURCJ B4ECY9_BURCJ] 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]


Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID)
==See Also==
 
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
Description: X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Glycine
__TOC__
</StructureSection>
[[Category: Burkholderia cenocepacia J2315]]
[[Category: Large Structures]]

Latest revision as of 17:18, 20 September 2023

X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Glycine

4otl, resolution 2.00Å

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