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3cuv
From Proteopedia
(Difference between revisions)
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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 [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:// | + | <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> |
| - | </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> | + | </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> |
<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> | <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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cut|3cut]], [[3cuu|3cuu]], [[3cuw|3cuw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cut|3cut]], [[3cuu|3cuu]], [[3cuw|3cuw]]</td></tr> | ||
<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> | <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> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <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> |
</table> | </table> | ||
== Function == | == Function == | ||
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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: Phosphorylase]] | [[Category: Phosphorylase]] | ||
Revision as of 10:29, 12 August 2020
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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Categories: Large Structures | Oryctolagus cuniculus | Phosphorylase | Chrysina, E D | Kyritsi, C | Leonidas, D D | Oikonomakos, N G | Zographos, S E | Acetylation | Allosteric enzyme | Carbohydrate metabolism | Catalytic site | Glycogen metabolism | Glycogen phosphorylase | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Pyridoxal phosphate | Rational inhibitor design | Transferase
