3u2t
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese== | ==Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese== | ||
<StructureSection load='3u2t' size='340' side='right' caption='[[3u2t]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='3u2t' size='340' side='right' caption='[[3u2t]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3u2t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3u2t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2T FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]], [[3u2u|3u2u]], [[3u2v|3u2v]], [[3u2w|3u2w]], [[3u2x|3u2x]]</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]], [[3u2u|3u2u]], [[3u2v|3u2v]], [[3u2w|3u2w]], [[3u2x|3u2x]]</td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG, GYG1 ([http://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'>[http://en.wikipedia.org/wiki/Glycogenin_glucosyltransferase Glycogenin glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.186 2.4.1.186] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycogenin_glucosyltransferase Glycogenin glucosyltransferase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2t RCSB], [http://www.ebi.ac.uk/pdbsum/3u2t 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=3u2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2t OCA], [http://pdbe.org/3u2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3u2t RCSB], [http://www.ebi.ac.uk/pdbsum/3u2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3u2t ProSAT]</span></td></tr> |
</table> | </table> | ||
+ | == Disease == | ||
+ | [[http://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 == | ||
+ | [[http://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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3u2t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Glycogenin glucosyltransferase]] | [[Category: Glycogenin glucosyltransferase]] | ||
- | [[Category: | + | [[Category: Human]] |
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] |
Revision as of 19:11, 10 December 2016
Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese
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Categories: Glycogenin glucosyltransferase | Human | 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