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3mrv

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==Glycogen phosphorylase complexed with 3-hydroxybenzaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==
==Glycogen phosphorylase complexed with 3-hydroxybenzaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone==
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<StructureSection load='3mrv' size='340' side='right' caption='[[3mrv]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
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<StructureSection load='3mrv' size='340' side='right'caption='[[3mrv]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3mrv]] is a 1 chain structure with 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=3MRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MRV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3mrv]] 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=3MRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MRV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=16F:N-({(2Z)-2-[(3-HYDROXYPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>16F</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
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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]] 1.94&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=16F:N-({(2Z)-2-[(3-HYDROXYPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>16F</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mqf|3mqf]], [[3mrt|3mrt]], [[3mrx|3mrx]], [[3ms2|3ms2]], [[3ms4|3ms4]], [[3ms7|3ms7]], [[3msc|3msc]], [[3mt7|3mt7]], [[3mt8|3mt8]], [[3mt9|3mt9]], [[3mta|3mta]], [[3mtb|3mtb]], [[3mtd|3mtd]]</td></tr>
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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=3mrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrv OCA], [https://pdbe.org/3mrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mrv RCSB], [https://www.ebi.ac.uk/pdbsum/3mrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mrv ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mrv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mrv RCSB], [http://www.ebi.ac.uk/pdbsum/3mrv PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3mrv" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
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*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
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[[Category: Alexacou K-M]]
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[[Category: Alexacou, K M]]
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[[Category: Glycogenolysis]]
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[[Category: Transferase-transferase inhibitor complex]]
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[[Category: Type 2 diabetes]]
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Current revision

Glycogen phosphorylase complexed with 3-hydroxybenzaldehyde-4-(beta-D-glucopyranosyl) thiosemicarbazone

PDB ID 3mrv

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