3u2x

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Current revision (13:46, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3u2x' size='340' side='right'caption='[[3u2x]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='3u2x' size='340' side='right'caption='[[3u2x]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U2X 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=ASO:1,5-ANHYDROSORBITOL'>ASO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 1.77&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3qvb|3qvb]], [[3q4s|3q4s]], [[3rmw|3rmw]], [[3rmv|3rmv]], [[3t7m|3t7m]], [[3t7o|3t7o]], [[3t7n|3t7n]], [[3u2t|3u2t]], [[3u2u|3u2u]], [[3u2v|3u2v]], [[3u2w|3u2w]]</div></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=ASO:1,5-ANHYDROSORBITOL'>ASO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycogenin_glucosyltransferase Glycogenin glucosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.186 2.4.1.186] </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=3u2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2x OCA], [https://pdbe.org/3u2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2x RCSB], [https://www.ebi.ac.uk/pdbsum/3u2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2x ProSAT]</span></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=3u2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2x OCA], [https://pdbe.org/3u2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u2x RCSB], [https://www.ebi.ac.uk/pdbsum/3u2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2x ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN]] Glycogen storage disease due to glycogenin deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN] Glycogen storage disease due to glycogenin deficiency. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN]] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
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[https://www.uniprot.org/uniprot/GLYG_HUMAN GLYG_HUMAN] Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Glycogenin glucosyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Chaikuad, A]]
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[[Category: Chaikuad A]]
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[[Category: Delft, F von]]
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[[Category: Edwards AM]]
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[[Category: Edwards, A M]]
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[[Category: Froese DS]]
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[[Category: Froese, D S]]
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[[Category: Krysztofinska E]]
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[[Category: Krysztofinska, E]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U]]
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[[Category: Weigelt J]]
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[[Category: Structural genomic]]
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[[Category: Yue WW]]
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[[Category: Weigelt, J]]
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[[Category: Von Delft F]]
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[[Category: Yue, W W]]
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[[Category: Glycogen biosynthesis]]
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[[Category: Glycosylation]]
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[[Category: Glycosyltransferase]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose

PDB ID 3u2x

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