5o54

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(New page: ==Glycogen Phosphorylase b in complex with 29a== <StructureSection load='5o54' size='340' side='right' caption='5o54, resolution 2.45&Aring;' scene=''> == Structural hi...)
Current revision (19:08, 29 November 2023) (edit) (undo)
 
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==Glycogen Phosphorylase b in complex with 29a==
==Glycogen Phosphorylase b in complex with 29a==
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<StructureSection load='5o54' size='340' side='right' caption='[[5o54]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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<StructureSection load='5o54' size='340' side='right'caption='[[5o54]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5o54]] 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=5O54 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O54 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5o54]] 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=5O54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O54 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9LB:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(5-phenyl-4~{H}-1,2,4-triazol-3-yl)oxane-3,4-diol'>9LB</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]] 2.45&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o50|5o50]], [[5o52|5o52]]</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=9LB:(2~{R},3~{S},4~{R},5~{R},6~{R})-5-azanyl-2-(hydroxymethyl)-6-(5-phenyl-4~{H}-1,2,4-triazol-3-yl)oxane-3,4-diol'>9LB</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=5o54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o54 OCA], [https://pdbe.org/5o54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o54 RCSB], [https://www.ebi.ac.uk/pdbsum/5o54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o54 ProSAT]</span></td></tr>
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<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=5o54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o54 OCA], [http://pdbe.org/5o54 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o54 RCSB], [http://www.ebi.ac.uk/pdbsum/5o54 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o54 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5o54" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5o54" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[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: Transferase]]
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Current revision

Glycogen Phosphorylase b in complex with 29a

PDB ID 5o54

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