3u2x: Difference between revisions

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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 ==
<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>
<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>
</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>
</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>
<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='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='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'>[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'>[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 ==
[[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.  
[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.  
[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>
[[Category: Glycogenin glucosyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Chaikuad, A]]
[[Category: Chaikuad A]]
[[Category: Delft, F von]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Froese DS]]
[[Category: Froese, D S]]
[[Category: Krysztofinska E]]
[[Category: Krysztofinska, E]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Weigelt J]]
[[Category: Structural genomic]]
[[Category: Yue WW]]
[[Category: Weigelt, J]]
[[Category: Von Delft F]]
[[Category: Yue, W W]]
[[Category: Glycogen biosynthesis]]
[[Category: Glycosylation]]
[[Category: Glycosyltransferase]]
[[Category: Sgc]]
[[Category: Transferase]]

Latest revision as of 16:46, 14 March 2024

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

Structural highlights

3u2x is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.77Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

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

GLYG_HUMAN Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.

See Also

3u2x, resolution 1.77Å

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