3ms4: Difference between revisions

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 ==Glycogen phosphorylase complexed with 4-trifluoromethylbenzaldehyde-4-(beta-D-glucopyranosyl)-thiosemicarbazone==
-<StructureSection load='3ms4' size='340' side='right' caption='[[3ms4]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
+<StructureSection load='3ms4' size='340' side='right'caption='[[3ms4]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ms4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MS4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ms4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MS4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=21N:N-{[(2E)-2-{[4-(TRIFLUOROMETHYL)PHENYL]METHYLIDENE}HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>21N</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]] 2.07&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=21N:N-{[(2E)-2-{[4-(TRIFLUOROMETHYL)PHENYL]METHYLIDENE}HYDRAZINO]CARBONOTHIOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>21N</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mqf|3mqf]], [[3mrt|3mrt]], [[3mrv|3mrv]], [[3mrx|3mrx]], [[3ms2|3ms2]], [[3ms7|3ms7]], [[3msc|3msc]], [[3mt7|3mt7]], [[3mt8|3mt8]], [[3mt9|3mt9]], [[3mta|3mta]], [[3mtb|3mtb]], [[3mtd|3mtd]]</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=3ms4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ms4 OCA], [https://pdbe.org/3ms4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ms4 RCSB], [https://www.ebi.ac.uk/pdbsum/3ms4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ms4 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/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=3ms4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ms4 OCA], [http://pdbe.org/3ms4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ms4 RCSB], [http://www.ebi.ac.uk/pdbsum/3ms4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ms4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
+[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 ==See Also==
-*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
+*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Phosphorylase]]
+[[Category: Alexacou K-M]]
-[[Category: Alexacou, K M]]
-[[Category: Glycogenolysis]]
-[[Category: Transferase-transferase inhibitor complex]]
-[[Category: Type 2 diabetes]]