4cto

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==Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods==
==Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods==
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<StructureSection load='4cto' size='340' side='right' caption='[[4cto]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='4cto' size='340' side='right'caption='[[4cto]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4cto]] 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=4CTO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CTO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4cto]] 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=4CTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CTO 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=M7C:N-[(2Z,5R,7R,8S,9S,10R)-8,9,10-TRIHYDROXY-7-(HYDROXYMETHYL)-4-OXO-6-OXA-1-THIA-3-AZASPIRO[4.5]DEC-2-YLIDENE]BENZAMIDE'>M7C</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ctm|4ctm]], [[4ctn|4ctn]]</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=M7C:N-[(2Z,5R,7R,8S,9S,10R)-8,9,10-TRIHYDROXY-7-(HYDROXYMETHYL)-4-OXO-6-OXA-1-THIA-3-AZASPIRO[4.5]DEC-2-YLIDENE]BENZAMIDE'>M7C</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4cto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cto OCA], [https://pdbe.org/4cto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cto RCSB], [https://www.ebi.ac.uk/pdbsum/4cto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cto ProSAT]</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=4cto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cto OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cto RCSB], [http://www.ebi.ac.uk/pdbsum/4cto 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 4cto" style="background-color:#fffaf0;"></div>
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==See Also==
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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 KM]]
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[[Category: Alexacou, K M]]
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[[Category: Chrysina ED]]
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[[Category: Chrysina, E D]]
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[[Category: Leonidas DD]]
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[[Category: Leonidas, D D]]
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[[Category: Papakonstantinou M]]
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[[Category: Papakonstantinou, M]]
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[[Category: Zographos SE]]
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[[Category: Zographos, S E]]
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[[Category: Inhibitor]]
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[[Category: Structure-based drug design]]
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[[Category: Transferase]]
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[[Category: Type 2 diabetes]]
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Current revision

Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods

PDB ID 4cto

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