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4m8g

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==Crystal structure of Se-Met hN33/Tusc3==
==Crystal structure of Se-Met hN33/Tusc3==
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<StructureSection load='4m8g' size='340' side='right' caption='[[4m8g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='4m8g' size='340' side='right'caption='[[4m8g]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4m8g]] 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=4M8G OCA]. <br>
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<table><tr><td colspan='2'>[[4m8g]] 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=4M8G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M8G FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m90|4m90]], [[4m91|4m91]], [[4m92|4m92]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8g OCA], [https://pdbe.org/4m8g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m8g RCSB], [https://www.ebi.ac.uk/pdbsum/4m8g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m8g ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N33, TUSC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m8g RCSB], [http://www.ebi.ac.uk/pdbsum/4m8g PDBsum]</span></td></tr>
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<table>
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== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref>
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[https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145<ref>PMID:24685145</ref>
Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145<ref>PMID:24685145</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4m8g" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Aebi, M.]]
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[[Category: Large Structures]]
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[[Category: Brozzo, M S.]]
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[[Category: Aebi M]]
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[[Category: Glockshuber, R.]]
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[[Category: Brozzo MS]]
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[[Category: Malojcic, G.]]
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[[Category: Glockshuber R]]
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[[Category: Mohorko, E.]]
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[[Category: Malojcic G]]
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[[Category: Owen, R L.]]
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[[Category: Mohorko E]]
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[[Category: Oxidoreductase]]
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[[Category: Owen RL]]
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[[Category: Redox-active protein]]
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[[Category: Thiol/disulfide exchange reaction]]
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[[Category: Thiol/disulfide oxidoreductase]]
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[[Category: Thioredoxin-like fold]]
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Current revision

Crystal structure of Se-Met hN33/Tusc3

PDB ID 4m8g

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