3mtb: Difference between revisions

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 <StructureSection load='3mtb' size='340' side='right'caption='[[3mtb]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mtb]] 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=3MTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MTB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mtb]] 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=3MTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MTB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=23V:N-({(2E)-2-[(3-CHLOROPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>23V</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]] 1.95&#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=23V:N-({(2E)-2-[(3-CHLOROPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>23V</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]], [[3ms4|3ms4]], [[3ms7|3ms7]], [[3msc|3msc]], [[3mt7|3mt7]], [[3mt8|3mt8]], [[3mt9|3mt9]], [[3mta|3mta]], [[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=3mtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtb OCA], [https://pdbe.org/3mtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mtb RCSB], [https://www.ebi.ac.uk/pdbsum/3mtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtb 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=3mtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mtb OCA], [http://pdbe.org/3mtb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mtb RCSB], [http://www.ebi.ac.uk/pdbsum/3mtb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mtb 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 30: / Line 28: @@
 [[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]]