3cuv

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Current revision (15:00, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3cuv' size='340' side='right'caption='[[3cuv]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='3cuv' size='340' side='right'caption='[[3cuv]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3cuv]] 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=3CUV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3CUV FirstGlance]. <br>
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<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>
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</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></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]] 1.93&#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:(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='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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cut|3cut]], [[3cuu|3cuu]], [[3cuw|3cuw]]</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=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>
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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://proteopedia.org/fgij/fg.htm?mol=3cuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cuv OCA], [http://pdbe.org/3cuv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cuv RCSB], [http://www.ebi.ac.uk/pdbsum/3cuv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cuv ProSAT]</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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
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[[Category: Chrysina ED]]
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[[Category: Chrysina, E D]]
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[[Category: Kyritsi C]]
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[[Category: Kyritsi, C]]
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[[Category: Leonidas DD]]
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[[Category: Leonidas, D D]]
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[[Category: Oikonomakos NG]]
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[[Category: Oikonomakos, N G]]
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[[Category: Zographos SE]]
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[[Category: Zographos, S E]]
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[[Category: Acetylation]]
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[[Category: Allosteric enzyme]]
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[[Category: Carbohydrate metabolism]]
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[[Category: Catalytic site]]
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[[Category: Glycogen metabolism]]
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[[Category: Glycogen phosphorylase]]
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[[Category: Glycosyltransferase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Rational inhibitor design]]
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[[Category: Transferase]]
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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

PDB ID 3cuv

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