3cuv
From Proteopedia
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==Tracking structure activity relationships of glycogen phosphorylase inhibitors: synthesis, kinetic and crystallographic evaluation of analogues of N-(-D-glucopyranosyl)-N'-oxamides== | ==Tracking structure activity relationships of glycogen phosphorylase inhibitors: synthesis, kinetic and crystallographic evaluation of analogues of N-(-D-glucopyranosyl)-N'-oxamides== | ||
| - | <StructureSection load='3cuv' size='340' side='right' caption='[[3cuv]], [[Resolution|resolution]] 1.93Å' scene=''> | + | <StructureSection load='3cuv' size='340' side='right'caption='[[3cuv]], [[Resolution|resolution]] 1.93Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3cuv]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3cuv]] 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=3CUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CUV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=475:N-[OXO(PYRIDIN-2-YLAMINO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>475</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=475:N-[OXO(PYRIDIN-2-YLAMINO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>475</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> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuv OCA], [https://pdbe.org/3cuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cuv RCSB], [https://www.ebi.ac.uk/pdbsum/3cuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cuv ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Glycogen | + | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | + | [[Category: Chrysina ED]] | |
| - | [[Category: Chrysina | + | [[Category: Kyritsi C]] |
| - | [[Category: Kyritsi | + | [[Category: Leonidas DD]] |
| - | [[Category: Leonidas | + | [[Category: Oikonomakos NG]] |
| - | [[Category: Oikonomakos | + | [[Category: Zographos SE]] |
| - | [[Category: Zographos | + | |
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Current revision
Tracking structure activity relationships of glycogen phosphorylase inhibitors: synthesis, kinetic and crystallographic evaluation of analogues of N-(-D-glucopyranosyl)-N'-oxamides
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