1fc0

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Current revision (06:03, 9 August 2023) (edit) (undo)
 
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<StructureSection load='1fc0' size='340' side='right'caption='[[1fc0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1fc0' size='340' side='right'caption='[[1fc0]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1fc0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FC0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1fc0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FC0 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=NBG:1-N-ACETYL-BETA-D-GLUCOSAMINE'>NBG</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]] 2.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fa9|1fa9]]</div></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=NBG:1-N-ACETYL-BETA-D-GLUCOSAMINE'>NBG</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'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://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=1fc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc0 OCA], [https://pdbe.org/1fc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fc0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fc0 OCA], [https://pdbe.org/1fc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fc0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fc0 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/PYGL_HUMAN PYGL_HUMAN]] Defects in PYGL are the cause of glycogen storage disease type 6 (GSD6) [MIM:[https://omim.org/entry/232700 232700]]. A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected.<ref>PMID:9529348</ref>
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[https://www.uniprot.org/uniprot/PYGL_HUMAN PYGL_HUMAN] Defects in PYGL are the cause of glycogen storage disease type 6 (GSD6) [MIM:[https://omim.org/entry/232700 232700]. A metabolic disorder characterized by mild to moderate hypoglycemia, mild ketosis, growth retardation, and prominent hepatomegaly. Heart and skeletal muscle are not affected.<ref>PMID:9529348</ref>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PYGL_HUMAN PYGL_HUMAN]] 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/PYGL_HUMAN PYGL_HUMAN] 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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphorylase]]
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[[Category: Ammirati M]]
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[[Category: Ammirati, M]]
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[[Category: Danley DE]]
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[[Category: Danley, D E]]
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[[Category: Fennell KF]]
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[[Category: Fennell, K F]]
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[[Category: Hynes TR]]
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[[Category: Hynes, T R]]
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[[Category: LeMotte PK]]
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[[Category: LeMotte, P K]]
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[[Category: Mansour MM]]
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[[Category: Mansour, M M]]
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[[Category: Pandit J]]
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[[Category: Pandit, J]]
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[[Category: Rath VL]]
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[[Category: Rath, V L]]
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[[Category: Schulte GK]]
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[[Category: Schulte, G K]]
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[[Category: Wasilko DJ]]
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[[Category: Wasilko, D J]]
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[[Category: Allosteric]]
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[[Category: Glucose analog]]
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[[Category: Inhibitor]]
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[[Category: Phosphorylated protein]]
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[[Category: Transferase]]
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Current revision

HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE

PDB ID 1fc0

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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