4ueg: Difference between revisions

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<StructureSection load='4ueg' size='340' side='right'caption='[[4ueg]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='4ueg' size='340' side='right'caption='[[4ueg]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ueg]] is a 2 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=4UEG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UEG FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ueg]] 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=4UEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UEG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4ueg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ueg OCA], [https://pdbe.org/4ueg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ueg RCSB], [https://www.ebi.ac.uk/pdbsum/4ueg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ueg ProSAT]</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=4ueg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ueg OCA], [http://pdbe.org/4ueg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ueg RCSB], [http://www.ebi.ac.uk/pdbsum/4ueg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ueg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GLYG2_HUMAN GLYG2_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/GLYG2_HUMAN GLYG2_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]]
[[Category: Arrowsmith C]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Burgess-Brown, N]]
[[Category: Burgess-Brown N]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Fairhead M]]
[[Category: Fairhead, M]]
[[Category: Froese DS]]
[[Category: Froese, D S]]
[[Category: Kopec J]]
[[Category: Kopec, J]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Nowak R]]
[[Category: Nowak, R]]
[[Category: Strain-Damerell C]]
[[Category: Strain-Damerell, C]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Glycogen biosynthesis]]
[[Category: Glycosylation]]
[[Category: Transferase]]

Revision as of 08:20, 22 March 2023

Crystal structure of human glycogenin-2 catalytic domain

4ueg, resolution 1.93Å

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