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2vi8

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<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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<table><tr><td colspan='2'>[[2vi8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VI8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VI8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vi8]] 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=2VI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VI8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
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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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 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>
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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=2vi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vi8 OCA], [https://pdbe.org/2vi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vi8 RCSB], [https://www.ebi.ac.uk/pdbsum/2vi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vi8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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>
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</table>
</table>
== Function ==
== Function ==
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[[http://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]
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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]]
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==See Also==
==See Also==
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*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]]
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*[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 12980]]
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[[Category: Geobacillus stearothermophilus]]
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[[Category: Glycine hydroxymethyltransferase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhavani, B S]]
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[[Category: Appaji Rao N]]
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[[Category: Murthy, M R.N]]
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[[Category: Bhavani BS]]
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[[Category: Prakash, V]]
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[[Category: Murthy MRN]]
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[[Category: Rajaram, V]]
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[[Category: Prakash V]]
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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: E53q]]
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[[Category: Enzyme memory]]
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[[Category: Fthf]]
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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: Shmt]]
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[[Category: Transferase]]
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Current revision

Crystal structure of S172AbsSHMT internal aldimine

PDB ID 2vi8

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