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2vmu

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==CRYSTAL STRUCTURE OF Y60ABSSHMT CRYSTALLIZED IN THE PRESENCE OF L-ALLO-THR==
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<StructureSection load='2vmu' size='340' side='right' caption='[[2vmu]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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==Crystal structure of Y60AbsSHMT crystallized in the presence of L- allo-Thr==
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<StructureSection load='2vmu' size='340' side='right'caption='[[2vmu]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vmu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VMU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VMU FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yjy|1yjy]], [[1kl2|1kl2]], [[2vib|2vib]], [[2vgs|2vgs]], [[1yjz|1yjz]], [[2vgv|2vgv]], [[2vgu|2vgu]], [[1yjs|1yjs]], [[2vi9|2vi9]], [[1kl1|1kl1]], [[2vi8|2vi8]], [[1kkp|1kkp]], [[2vgt|2vgt]], [[2via|2via]], [[1kkj|1kkj]], [[2vgw|2vgw]], [[2vmp|2vmp]], [[2vmr|2vmr]], [[2vmv|2vmv]], [[2vmq|2vmq]], [[2vms|2vms]], [[2vmt|2vmt]], [[2vmw|2vmw]], [[2vmn|2vmn]], [[2vmx|2vmx]], [[2vmo|2vmo]], [[2vmy|2vmy]], [[2vmz|2vmz]]</td></tr>
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<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>
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<tr><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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmu OCA], [https://pdbe.org/2vmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vmu RCSB], [https://www.ebi.ac.uk/pdbsum/2vmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vmu ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vmu RCSB], [http://www.ebi.ac.uk/pdbsum/2vmu PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vmu_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vm/2vmu_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>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vmu ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2vmu" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]]
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*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Glycine hydroxymethyltransferase]]
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[[Category: Large Structures]]
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[[Category: Bhavani, B S.]]
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[[Category: Appaji Rao N]]
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[[Category: Bisht, S.]]
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[[Category: Bhavani BS]]
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[[Category: Murthy, M R.N.]]
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[[Category: Bisht S]]
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[[Category: Pai, V R.]]
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[[Category: Murthy MRN]]
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[[Category: Rajaram, V.]]
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[[Category: Pai VR]]
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[[Category: Rao, N Appaji.]]
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[[Category: Rajaram V]]
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[[Category: Savithri, H S.]]
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[[Category: Savithri HS]]
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[[Category: Folate binding]]
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[[Category: One-carbon metabolism]]
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[[Category: Plp-dependent enzyme]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Serine hydroxymethyltransferase]]
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[[Category: Shmt]]
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[[Category: Transferase]]
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[[Category: Y60a]]
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Current revision

Crystal structure of Y60AbsSHMT crystallized in the presence of L- allo-Thr

PDB ID 2vmu

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