3u2x
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose== | ==Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose== | ||
| - | <StructureSection load='3u2x' size='340' side='right' caption='[[3u2x]], [[Resolution|resolution]] 1.77Å' scene=''> | + | <StructureSection load='3u2x' size='340' side='right'caption='[[3u2x]], [[Resolution|resolution]] 1.77Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3u2x]] is a 2 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </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> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qvb|3qvb]], [[3q4s|3q4s]], [[3rmw|3rmw]], [[3rmv|3rmv]], [[3t7m|3t7m]], [[3t7o|3t7o]], [[3t7n|3t7n]], [[3u2t|3u2t]], [[3u2u|3u2u]], [[3u2v|3u2v]], [[3u2w|3u2w]]</td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([ | + | <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> |
| - | <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/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> |
| - | <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=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 == | ||
| - | [[ | + | [[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 == | ||
| - | [[ | + | [[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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[[Category: Glycogenin glucosyltransferase]] | [[Category: Glycogenin glucosyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
Revision as of 05:55, 13 July 2022
Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and 1'-deoxyglucose
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Categories: Glycogenin glucosyltransferase | Human | Large Structures | Arrowsmith, C H | Bountra, C | Chaikuad, A | Delft, F von | Edwards, A M | Froese, D S | Krysztofinska, E | Oppermann, U | Structural genomic | Weigelt, J | Yue, W W | Glycogen biosynthesis | Glycosylation | Glycosyltransferase | Sgc | Transferase
