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6r0h
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Glycogen Phosphorylase b in complex with 3== | |
| - | + | <StructureSection load='6r0h' size='340' side='right'caption='[[6r0h]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6r0h]] 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=6R0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R0H FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JN2:3-(4-fluorophenyl)-~{N}-[(2~{R},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]benzamide'>JN2</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |
| - | [[Category: | + | <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> |
| + | <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=6r0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0h OCA], [http://pdbe.org/6r0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0h RCSB], [http://www.ebi.ac.uk/pdbsum/6r0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Phosphorylase]] | ||
| + | [[Category: Koulas, M S]] | ||
[[Category: Kyriakis, E]] | [[Category: Kyriakis, E]] | ||
| - | [[Category: | + | [[Category: Leonidas, D D]] |
| - | [[Category: Skamnaki, V | + | [[Category: Skamnaki, V T]] |
| - | [[Category: | + | [[Category: Stravodimos, G A]] |
| - | [[Category: | + | [[Category: Tsagkarakou, S A]] |
| - | [[Category: | + | [[Category: Transferase]] |
Revision as of 07:31, 10 April 2019
Glycogen Phosphorylase b in complex with 3
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