2qn3: Difference between revisions

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[[Image:2qn3.jpg|left|200px]]


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==Glycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl urea==
The line below this paragraph, containing "STRUCTURE_2qn3", creates the "Structure Box" on the page.
<StructureSection load='2qn3' size='340' side='right'caption='[[2qn3]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2qn3| PDB=2qn3 |  SCENE= }}
<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>


===Glycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl urea===
==See Also==
 
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
2QN3 is a [[Single protein]] structure of 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=2QN3 OCA].
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Alexacou K-M]]
[[Category: Single protein]]
[[Category: Chrysina ED]]
[[Category: Alexacou, K M.]]
[[Category: Leonidas DD]]
[[Category: Chrysina, E D.]]
[[Category: Oikonomakos NG]]
[[Category: Leonidas, D D.]]
[[Category: Tiraidis C]]
[[Category: Oikonomakos, N G.]]
[[Category: Zographos SE]]
[[Category: Tiraidis, C.]]
[[Category: Zographos, S E.]]
[[Category: Acetylation]]
[[Category: Allosteric enzyme]]
[[Category: Carbohydrate metabolism]]
[[Category: Glycogen metabolism]]
[[Category: Glycogenolysis]]
[[Category: Glycosyltransferase]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Pyridoxal phosphate]]
[[Category: Transferase]]
[[Category: Type 2 diabetes]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 23 11:36:05 2008''

Latest revision as of 14:36, 30 August 2023

Glycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl ureaGlycogen Phosphorylase in complex with N-4-chlorobenzoyl-N-beta-D-glucopyranosyl urea

Structural highlights

2qn3 is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.96Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2qn3, resolution 1.96Å

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OCA
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