1axr

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[[Image:1axr.gif|left|200px]]
 
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{{Structure
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==COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B==
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|PDB= 1axr |SIZE=350|CAPTION= <scene name='initialview01'>1axr</scene>, resolution 2.3&Aring;
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<StructureSection load='1axr' size='340' side='right'caption='[[1axr]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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&#39;-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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<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>
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|ACTIVITY= <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>
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</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>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axr OCA], [http://www.ebi.ac.uk/pdbsum/1axr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1axr RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ax/1axr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''COOPERATIVITY BETWEEN HYDROGEN-BONDING AND CHARGE-DIPOLE INTERACTIONS IN THE INHIBITION OF BETA-GLYCOSIDASES BY AZOLOPYRIDINES: EVIDENCE FROM A STUDY WITH GLYCOGEN PHOSPHORYLASE B'''
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==See Also==
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*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
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__TOC__
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==About this Structure==
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</StructureSection>
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1AXR 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=1AXR OCA].
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
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[[Category: Heightman TD]]
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[[Category: Single protein]]
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[[Category: Oikonomakos NG]]
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[[Category: Heightman, T D.]]
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[[Category: Oikonomakos, N G.]]
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[[Category: azolopyridine]]
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[[Category: catalytic mechanism]]
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[[Category: glycogen phosphorylase]]
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[[Category: glycosidase]]
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[[Category: inhibitor]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:33 2008''
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Current revision

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

PDB ID 1axr

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