2vmq: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='2vmq' size='340' side='right'caption='[[2vmq]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='2vmq' size='340' side='right'caption='[[2vmq]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vmq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2vmq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VMQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kkj|1kkj]], [[1kkp|1kkp]], [[1kl1|1kl1]], [[1yjy|1yjy]], [[1yjz|1yjz]], [[2vgs|2vgs]], [[2vgu|2vgu]], [[2vi8|2vi8]], [[2vi9|2vi9]], [[2via|2via]], [[2vib|2vib]], [[1kl2|1kl2]], [[1yjs|1yjs]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[2vgw|2vgw]], [[2vmn|2vmn]], [[2vmo|2vmo]], [[2vmp|2vmp]], [[2vmr|2vmr]], [[2vms|2vms]], [[2vmt|2vmt]], [[2vmu|2vmu]], [[2vmv|2vmv]], [[2vmw|2vmw]], [[2vmx|2vmx]], [[2vmy|2vmy]], [[2vmz|2vmz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1kkj|1kkj]], [[1kkp|1kkp]], [[1kl1|1kl1]], [[1yjy|1yjy]], [[1yjz|1yjz]], [[2vgs|2vgs]], [[2vgu|2vgu]], [[2vi8|2vi8]], [[2vi9|2vi9]], [[2via|2via]], [[2vib|2vib]], [[1kl2|1kl2]], [[1yjs|1yjs]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[2vgw|2vgw]], [[2vmn|2vmn]], [[2vmo|2vmo]], [[2vmp|2vmp]], [[2vmr|2vmr]], [[2vms|2vms]], [[2vmt|2vmt]], [[2vmu|2vmu]], [[2vmv|2vmv]], [[2vmw|2vmw]], [[2vmx|2vmx]], [[2vmy|2vmy]], [[2vmz|2vmz]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmq OCA], [https://pdbe.org/2vmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vmq RCSB], [https://www.ebi.ac.uk/pdbsum/2vmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/Q7SIB6_GEOSE Q7SIB6_GEOSE]] 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]] | ||
Line 32: | Line 32: | ||
==See Also== | ==See Also== | ||
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> |