2gpn: Difference between revisions
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==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION== | ==100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION== | ||
<StructureSection load='2gpn' size='340' side='right' caption='[[2gpn]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='2gpn' size='340' side='right'caption='[[2gpn]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gpn]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2gpn]] 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=2GPN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GPN 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]] 1.99Å</td></tr> | ||
<tr id=' | <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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gpn OCA], [https://pdbe.org/2gpn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gpn RCSB], [https://www.ebi.ac.uk/pdbsum/2gpn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gpn ProSAT]</span></td></tr> | ||
</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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==See Also== | ==See Also== | ||
*[[Glycogen | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: | [[Category: De La Fuente C]] | ||
[[Category: Fleet | [[Category: Fleet GWJ]] | ||
[[Category: Garman EF]] | |||
[[Category: Garman | [[Category: Gregoriou M]] | ||
[[Category: Gregoriou | [[Category: Johnson LN]] | ||
[[Category: Johnson | [[Category: Krulle TM]] | ||
[[Category: Krulle | [[Category: Noble MEM]] | ||
[[Category: Noble | [[Category: Oikonomakos NG]] | ||
[[Category: Oikonomakos | [[Category: Watson KA]] | ||
[[Category: Watson | |||