5o50

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Current revision (19:08, 29 November 2023) (edit) (undo)
 
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<StructureSection load='5o50' size='340' side='right'caption='[[5o50]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5o50' size='340' side='right'caption='[[5o50]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5o50]] 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=5O50 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O50 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5o50]] 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=5O50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O50 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=9L2:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-phenyl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9L2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.9&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9L2:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(4-phenyl-1~{H}-imidazol-2-yl)oxane-3,4-diol'>9L2</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=5o50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o50 OCA], [http://pdbe.org/5o50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o50 RCSB], [http://www.ebi.ac.uk/pdbsum/5o50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o50 ProSAT]</span></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=5o50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o50 OCA], [https://pdbe.org/5o50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o50 RCSB], [https://www.ebi.ac.uk/pdbsum/5o50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o50 ProSAT]</span></td></tr>
</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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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: Chatzileontiadou DS]]
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[[Category: Chatzileontiadou, D S]]
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[[Category: Kantsadi AL]]
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[[Category: Kantsadi, A L]]
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[[Category: Kyriakis E]]
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[[Category: Kyriakis, E]]
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[[Category: Leonidas DD]]
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[[Category: Leonidas, D D]]
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[[Category: Skamnaki VT]]
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[[Category: Skamnaki, V T]]
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[[Category: Solovou TGA]]
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[[Category: Solovou, T G.A]]
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[[Category: Stravodimos GA]]
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[[Category: Stravodimos, G A]]
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[[Category: Alpha and beta protein]]
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[[Category: Transferase]]
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Current revision

Glycogen Phosphorylase b in complex with 33a

PDB ID 5o50

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OCA

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