3h7f

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h7f RCSB], [http://www.ebi.ac.uk/pdbsum/3h7f PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3h7f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h7f RCSB], [http://www.ebi.ac.uk/pdbsum/3h7f PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GLYA1_MYCTU GLYA1_MYCTU]] 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. Thus, is able to catalyze the cleavage of L-allo-threonine.<ref>PMID:12913008</ref>
== 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==
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]]
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 21:32, 24 December 2014

Crystal structure of serine hydroxymethyltransferase from Mycobacterium tuberculosis

3h7f, resolution 1.50Å

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