3bda: Difference between revisions
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<StructureSection load='3bda' size='340' side='right'caption='[[3bda]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3bda' size='340' side='right'caption='[[3bda]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bda]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3bda]] 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=3BDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BDA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C4B:1-BETA-D-GLUCOPYRANOSYL-1,3,5-TRIAZINANE-2,4,6-TRIONE'>C4B</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=3bda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bda OCA], [https://pdbe.org/3bda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bda RCSB], [https://www.ebi.ac.uk/pdbsum/3bda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bda ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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]] | ||
[[Category: Chrysina ED]] | |||
[[Category: Chrysina | [[Category: Hadjiloi T]] | ||
[[Category: Hadjiloi | [[Category: Hayes JM]] | ||
[[Category: Hayes | [[Category: Oikonomakos NG]] | ||
[[Category: Oikonomakos | [[Category: Sovantzis DA]] | ||
[[Category: Sovantzis | [[Category: Zographos SE]] | ||
[[Category: Zographos | |||
Latest revision as of 17:44, 1 November 2023
Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) cyanuric acidGlycogen Phosphorylase complex with 1(-D-glucopyranosyl) cyanuric acid
Structural highlights
FunctionPYGM_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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