3cut
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==Crystal structure of glycogen phosphorylase b in complex with N-(-D-glucopyranosyl)-N'-(2-naphthyl)oxamide== | ==Crystal structure of glycogen phosphorylase b in complex with N-(-D-glucopyranosyl)-N'-(2-naphthyl)oxamide== | ||
<StructureSection load='3cut' size='340' side='right' caption='[[3cut]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3cut' size='340' side='right' caption='[[3cut]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cut]] 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=3CUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUT FirstGlance]. <br> | <table><tr><td colspan='2'>[[3cut]] 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=3CUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUT FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=179:N-[(NAPHTHALEN-2-YLAMINO)(OXO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>179</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=179:N-[(NAPHTHALEN-2-YLAMINO)(OXO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>179</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2- | + | <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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cuu|3cuu]], [[3cuv|3cuv]], [[3cuw|3cuw]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cuu|3cuu]], [[3cuv|3cuv]], [[3cuw|3cuw]]</td></tr> |
| - | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cut RCSB], [http://www.ebi.ac.uk/pdbsum/3cut PDBsum]</span></td></tr> | + | <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=3cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cut OCA], [http://pdbe.org/3cut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cut RCSB], [http://www.ebi.ac.uk/pdbsum/3cut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cut ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cut ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
| - | [[Category: Chrysina, E D | + | [[Category: Chrysina, E D]] |
| - | [[Category: Kyritsi, C | + | [[Category: Kyritsi, C]] |
| - | [[Category: Leonidas, D D | + | [[Category: Leonidas, D D]] |
| - | [[Category: Oikonomakos, N G | + | [[Category: Oikonomakos, N G]] |
| - | [[Category: Zographos, S E | + | [[Category: Zographos, S E]] |
[[Category: Allosteric enzyme]] | [[Category: Allosteric enzyme]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
Current revision
Crystal structure of glycogen phosphorylase b in complex with N-(-D-glucopyranosyl)-N'-(2-naphthyl)oxamide
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Categories: Oryctolagus cuniculus | Phosphorylase | Chrysina, E D | Kyritsi, C | Leonidas, D D | Oikonomakos, N G | Zographos, S E | Allosteric enzyme | Carbohydrate metabolism | Catalytic site | Glycogen metabolism | Glycogen phosphorylase | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Pyridoxal phosphate | Rational inhibitor design | Transferase
