1ftq: Difference between revisions

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 ==STRUCTURES OF GLYCOGEN PHOSPHORYLASE-INHIBITOR COMPLEXES AND THE IMPLICATIONS FOR STRUCTURE-BASED DRUG DESIGN==
-<StructureSection load='1ftq' size='340' side='right' caption='[[1ftq]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+<StructureSection load='1ftq' size='340' side='right'caption='[[1ftq]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ftq]] 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=1FTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FTQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ftq]] 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=1FTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FTQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GL2:3-AMINO-8,9,10-TRIHYDROXY-7-HYDROXYMETHYL-6-OXA-1,3-DIAZA-SPIRO[4.5]DECANE-2,4-DIONE'>GL2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.35&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b4d|1b4d]], [[1ggn|1ggn]], [[1fs4|1fs4]], [[1ftw|1ftw]], [[1fty|1fty]], [[1fu4|1fu4]], [[1fu7|1fu7]], [[1fu8|1fu8]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GL2:3-AMINO-8,9,10-TRIHYDROXY-7-HYDROXYMETHYL-6-OXA-1,3-DIAZA-SPIRO[4.5]DECANE-2,4-DIONE'>GL2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1ftq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ftq OCA], [https://pdbe.org/1ftq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ftq RCSB], [https://www.ebi.ac.uk/pdbsum/1ftq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ftq ProSAT]</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=1ftq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ftq OCA], [http://pdbe.org/1ftq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ftq RCSB], [http://www.ebi.ac.uk/pdbsum/1ftq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ftq 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </div>
 <div class="pdbe-citations 1ftq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Phosphorylase]]
+[[Category: Fleet GW]]
-[[Category: Fleet, G W]]
+[[Category: Gregoriou M]]
-[[Category: Gregoriou, M]]
+[[Category: Johnson LN]]
-[[Category: Johnson, L N]]
+[[Category: Oikonomakos NG]]
-[[Category: Oikonomakos, N G]]
+[[Category: Skamnaki VT]]
-[[Category: Skamnaki, V T]]
+[[Category: Tsitsanou KE]]
-[[Category: Tsitsanou, K E]]
+[[Category: Watson KA]]
-[[Category: Watson, K A]]
+[[Category: Zographos SE]]
-[[Category: Zographos, S E]]
-[[Category: Catalytic site]]
-[[Category: Design]]
-[[Category: Glycogen phosphorylase]]
-[[Category: Inhibitor complex]]
-[[Category: Transferase]]