2qn3: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2qn3 is ON HOLD  until Paper Publication
+==Glycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl urea==
+<StructureSection load='2qn3' size='340' side='right'caption='[[2qn3]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2qn3]] 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=2QN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.96&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F55:N-{[(4-CHLOROPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>F55</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn3 OCA], [https://pdbe.org/2qn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/2qn3_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qn3 ConSurf].
+<div style="clear:both"></div>
-Authors: Chrysina, E.D., Tiraidis, C., Alexacou, K.-M., Zographos, S.E., Leonidas, D.D., Oikonomakos, N.G.
+==See Also==
+*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
-Description: Glycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl urea
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 08:38:07 2008''
+[[Category: Oryctolagus cuniculus]]
+[[Category: Alexacou K-M]]
+[[Category: Chrysina ED]]
+[[Category: Leonidas DD]]
+[[Category: Oikonomakos NG]]
+[[Category: Tiraidis C]]
+[[Category: Zographos SE]]