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==Complex structure of serine hydroxymethyltransferase from Enterococcus faecium and its inhibitor== | ==Complex structure of serine hydroxymethyltransferase from Enterococcus faecium and its inhibitor== | ||
<StructureSection load='7v3d' size='340' side='right'caption='[[7v3d]]' scene=''> | <StructureSection load='7v3d' size='340' side='right'caption='[[7v3d]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V3D FirstGlance]. <br> | <table><tr><td colspan='2'>[[7v3d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecium Enterococcus faecium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V3D FirstGlance]. <br> | ||
</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=7v3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v3d OCA], [https://pdbe.org/7v3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v3d RCSB], [https://www.ebi.ac.uk/pdbsum/7v3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v3d ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5M5:(4R)-6-azanyl-4-[3-(hydroxymethyl)-5-phenyl-phenyl]-3-methyl-4-propan-2-yl-1H-pyrano[2,3-c]pyrazole-5-carbonitrile'>5M5</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=7v3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v3d OCA], [https://pdbe.org/7v3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v3d RCSB], [https://www.ebi.ac.uk/pdbsum/7v3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v3d ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A133CK16_ENTFC A0A133CK16_ENTFC] 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] | |||
==See Also== | |||
*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Enterococcus faecium]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hayashi H]] | [[Category: Hayashi H]] | ||
[[Category: Murayama K]] | [[Category: Murayama K]] | ||
Latest revision as of 20:19, 29 November 2023
Complex structure of serine hydroxymethyltransferase from Enterococcus faecium and its inhibitorComplex structure of serine hydroxymethyltransferase from Enterococcus faecium and its inhibitor
Structural highlights
FunctionA0A133CK16_ENTFC 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] See Also |
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