2vi8: Difference between revisions

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==CRYSTAL STRUCTURE OF S172ABSSHMT INTERNAL ALDIMINE==
 
==Crystal structure of S172AbsSHMT internal aldimine==
<StructureSection load='2vi8' size='340' side='right' caption='[[2vi8]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='2vi8' size='340' side='right' caption='[[2vi8]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vgu|2vgu]], [[1yjy|1yjy]], [[1yjs|1yjs]], [[1kl2|1kl2]], [[1kl1|1kl1]], [[1kkp|1kkp]], [[2vgs|2vgs]], [[1yjz|1yjz]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[1kkj|1kkj]], [[2vgw|2vgw]], [[2vib|2vib]], [[2via|2via]], [[2vi9|2vi9]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vgu|2vgu]], [[1yjy|1yjy]], [[1yjs|1yjs]], [[1kl2|1kl2]], [[1kl1|1kl1]], [[1kkp|1kkp]], [[2vgs|2vgs]], [[1yjz|1yjz]], [[2vgt|2vgt]], [[2vgv|2vgv]], [[1kkj|1kkj]], [[2vgw|2vgw]], [[2vib|2vib]], [[2via|2via]], [[2vi9|2vi9]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.1 2.1.2.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_hydroxymethyltransferase Glycine hydroxymethyltransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi8 OCA], [http://pdbe.org/2vi8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vi8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vi8 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=2vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi8 OCA], [http://pdbe.org/2vi8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vi8 RCSB], [http://www.ebi.ac.uk/pdbsum/2vi8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vi8_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/2vi8_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 23:29, 19 September 2018

Crystal structure of S172AbsSHMT internal aldimineCrystal structure of S172AbsSHMT internal aldimine

Structural highlights

2vi8 is a 1 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Glycine hydroxymethyltransferase, with EC number 2.1.2.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2vi8, resolution 1.67Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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