3bd6

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Current revision (14:44, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3bd6' size='340' side='right'caption='[[3bd6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3bd6' size='340' side='right'caption='[[3bd6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bd6]] 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=3BD6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BD6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3bd6]] 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=3BD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BD6 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=RDD:1-BETA-D-RIBOFURANOSYL-1,3,5-TRIAZINANE-2,4,6-TRIONE'>RDD</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]] 2&#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=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=RDD:1-BETA-D-RIBOFURANOSYL-1,3,5-TRIAZINANE-2,4,6-TRIONE'>RDD</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bcr|3bcr]], [[3bcs|3bcs]], [[3bcu|3bcu]], [[3bd7|3bd7]], [[3bd8|3bd8]], [[3bda|3bda]]</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=3bd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd6 OCA], [https://pdbe.org/3bd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3bd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd6 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=3bd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd6 OCA], [http://pdbe.org/3bd6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bd6 RCSB], [http://www.ebi.ac.uk/pdbsum/3bd6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd6 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: Hadjiloi T]]
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[[Category: Hadjiloi, T]]
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[[Category: Hayes JM]]
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[[Category: Hayes, J M]]
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[[Category: Oikonomakos NG]]
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[[Category: Oikonomakos, N G]]
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[[Category: Sovantzis DA]]
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[[Category: Sovantzis, D A]]
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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: Glycogen metabolism]]
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[[Category: Glycogenolysis]]
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[[Category: Glycosyltransferase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphorylation]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Transferase]]
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[[Category: Type 2 diabetes]]
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Current revision

Glycogen Phosphorylase complex with 1(-D-ribofuranosyl) cyanuric acid

PDB ID 3bd6

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