1axr: Difference between revisions

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New page: left|200px<br /><applet load="1axr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1axr, resolution 2.3Å" /> '''COOPERATIVITY BETWEEN...
 
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[[Image:1axr.gif|left|200px]]<br /><applet load="1axr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1axr, resolution 2.3&Aring;" />
'''COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B'''<br />


==About this Structure==
==COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B==
1AXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PO4, PLP and HTP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AXR OCA].  
<StructureSection load='1axr' size='340' side='right'caption='[[1axr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1axr]] 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=1AXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXR 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HTP:4,5,6-TRIHYDROXY-7-HYDROXYMETHYL-4,5,6,7-TETRAHYDRO-1H-[1,2,3]TRIAZOLO[1,5-A]PYRIDIN-8-YLIUM'>HTP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1axr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axr OCA], [https://pdbe.org/1axr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axr RCSB], [https://www.ebi.ac.uk/pdbsum/1axr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axr 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/ax/1axr_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=1axr 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: Phosphorylase]]
[[Category: Heightman TD]]
[[Category: Single protein]]
[[Category: Oikonomakos NG]]
[[Category: Heightman, T.D.]]
[[Category: Oikonomakos, N.G.]]
[[Category: HTP]]
[[Category: PLP]]
[[Category: PO4]]
[[Category: azolopyridines]]
[[Category: catalytic mechanism]]
[[Category: glycogen phosphorylase]]
[[Category: glycosidases]]
[[Category: inhibitors]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:11:26 2007''

Latest revision as of 15:29, 13 March 2024

COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B

1axr, resolution 2.30Å

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