2qn9
From Proteopedia
(Difference between revisions)
| (11 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
| - | [[Image:2qn9.jpg|left|200px]] | ||
| - | + | ==Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea== | |
| - | + | <StructureSection load='2qn9' size='340' side='right'caption='[[2qn9]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2qn9]] 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=2QN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN9 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]] 2Å</td></tr> | |
| - | --> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=NBX:N-{[(4-AMINOPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>NBX</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=2qn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn9 OCA], [https://pdbe.org/2qn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn9 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn9 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/2qn9_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=2qn9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | + | [[Category: Alexacou K-M]] | |
| - | + | [[Category: Chrysina ED]] | |
| - | [[Category: Alexacou | + | [[Category: Leonidas DD]] |
| - | [[Category: Chrysina | + | [[Category: Oikonomakos NG]] |
| - | [[Category: Leonidas | + | [[Category: Tiraidis C]] |
| - | [[Category: Oikonomakos | + | [[Category: Zographos SE]] |
| - | [[Category: Tiraidis | + | |
| - | [[Category: Zographos | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea
| |||||||||||
