4xqm: Difference between revisions

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 ==Crystal structure of the MRH domain of Glucosidase II beta bound to mannose==
-<StructureSection load='4xqm' size='340' side='right' caption='[[4xqm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
+<StructureSection load='4xqm' size='340' side='right'caption='[[4xqm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4xqm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fission_yeast Fission yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XQM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4xqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XQM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 1.625&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2lvx|2lvx]], [[2n1h|2n1h]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gtb1, gls2-beta, SPCC825.02 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284812 Fission yeast])</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=4xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xqm OCA], [https://pdbe.org/4xqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xqm RCSB], [https://www.ebi.ac.uk/pdbsum/4xqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xqm 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/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.84 3.2.1.84] </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=4xqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xqm OCA], [http://pdbe.org/4xqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xqm RCSB], [http://www.ebi.ac.uk/pdbsum/4xqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xqm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLU2B_SCHPO GLU2B_SCHPO]] Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins in the endoplasmic reticulum (ER). Specifically required for the cleavage of the final glucose. The subunit beta retains the catalytic subunit alpha in the ER.<ref>PMID:10464333</ref> <ref>PMID:19605557</ref> <ref>PMID:21471007</ref>
+[https://www.uniprot.org/uniprot/GLU2B_SCHPO GLU2B_SCHPO] Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins in the endoplasmic reticulum (ER). Specifically required for the cleavage of the final glucose. The subunit beta retains the catalytic subunit alpha in the ER.<ref>PMID:10464333</ref> <ref>PMID:19605557</ref> <ref>PMID:21471007</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 19: @@
 </div>
 <div class="pdbe-citations 4xqm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Fission yeast]]
+[[Category: Large Structures]]
-[[Category: Hydrolase]]
+[[Category: Schizosaccharomyces pombe 972h-]]
-[[Category: Dahms, N M]]
+[[Category: Dahms NM]]
-[[Category: Kim, J J.P]]
+[[Category: Kim J-JP]]
-[[Category: Olson, L J]]
+[[Category: Olson LJ]]
-[[Category: Sugar binding protein]]