2pyi: Difference between revisions

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 ==Crystal structure of Glycogen Phosphorylase in complex with glucosyl triazoleacetamide==
-<StructureSection load='2pyi' size='340' side='right' caption='[[2pyi]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
+<StructureSection load='2pyi' size='340' side='right'caption='[[2pyi]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2pyi]] 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=2PYI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PYI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2pyi]] 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=2PYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PYI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DL8:N-[(4-PHENYL-1H-1,2,3-TRIAZOL-1-YL)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>DL8</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</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]] 1.88&#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=DL8:N-[(4-PHENYL-1H-1,2,3-TRIAZOL-1-YL)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>DL8</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</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">[[2pyd|2pyd]]</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=2pyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyi OCA], [https://pdbe.org/2pyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pyi RCSB], [https://www.ebi.ac.uk/pdbsum/2pyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyi 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=2pyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyi OCA], [http://pdbe.org/2pyi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pyi RCSB], [http://www.ebi.ac.uk/pdbsum/2pyi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyi 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]]
@@ Line 33: / Line 31: @@
 ==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 KM]]
-[[Category: Alexacou, K M]]
+[[Category: Chrysina ED]]
-[[Category: Chrysina, E D]]
+[[Category: Hayes J]]
-[[Category: Hayes, J]]
+[[Category: Oikonomakos NG]]
-[[Category: Oikonomakos, N G]]
+[[Category: Tiraidis C]]
-[[Category: Tiraidis, C]]
+[[Category: Zographos SE]]
-[[Category: Zographos, S E]]
-[[Category: Glycogenolysis]]
-[[Category: Inhibition]]
-[[Category: Transferase]]
-[[Category: Type 2 diabetes]]