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5vmb
From Proteopedia
(Difference between revisions)
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<StructureSection load='5vmb' size='340' side='right'caption='[[5vmb]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='5vmb' size='340' side='right'caption='[[5vmb]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5vmb]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5vmb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VMB FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=5vmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vmb OCA], [https://pdbe.org/5vmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vmb RCSB], [https://www.ebi.ac.uk/pdbsum/5vmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vmb ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/V5VBJ2_ACIBA V5VBJ2_ACIBA] 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== | ==See Also== | ||
| - | *[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | + | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acinetobacter baumannii]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Essentiallity screen]] | ||
| - | [[Category: Niaid]] | ||
| - | [[Category: Protein production]] | ||
| - | [[Category: Serine production]] | ||
| - | [[Category: Ssgcid]] | ||
| - | [[Category: Thf]] | ||
| - | [[Category: Transferase]] | ||
Current revision
Crystal structure of a glycine hydroxymethyltransferase from Acinetobacter baumannii
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