6eqj: Difference between revisions

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==Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant, apo form==
==Crystal Structure of Human Glycogenin-1 (GYG1) Tyr195pIPhe mutant, apo form==
<StructureSection load='6eqj' size='340' side='right' caption='[[6eqj]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
<StructureSection load='6eqj' size='340' side='right'caption='[[6eqj]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6eqj]] 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=6EQJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EQJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[6eqj]] is a 1 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=6EQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EQJ 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></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]] 2.18&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GYG1, GYG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6eqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqj OCA], [https://pdbe.org/6eqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eqj RCSB], [https://www.ebi.ac.uk/pdbsum/6eqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqj ProSAT]</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=6eqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eqj OCA], [http://pdbe.org/6eqj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eqj RCSB], [http://www.ebi.ac.uk/pdbsum/6eqj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eqj ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== 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.  
[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 ==
[[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.  
[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Glycogenin glucosyltransferase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bailey, H J]]
[[Category: Bailey HJ]]
[[Category: Bezerra, G A]]
[[Category: Bezerra GA]]
[[Category: Bilyard, M K]]
[[Category: Bilyard MK]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Davis, B G]]
[[Category: Davis BG]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Kopec, J]]
[[Category: Kopec J]]
[[Category: Lee, S Seo]]
[[Category: Seo Lee S]]
[[Category: Yue, W W]]
[[Category: Yue WW]]
[[Category: Glycogenin-1]]
[[Category: Hydrolase]]

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