6qa8
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Glycogen Phosphorylase b in complex with 28== | |
| - | + | <StructureSection load='6qa8' size='340' side='right'caption='[[6qa8]], [[Resolution|resolution]] 2.35Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6qa8]] 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=6QA8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QA8 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HTE:(5~{S},7~{R},8~{S},9~{S},10~{R})-7-(hydroxymethyl)-8,9,10-tris(oxidanyl)-2-phenyl-6-oxa-1,3-diazaspiro[4.5]dec-1-en-4-one'>HTE</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=6qa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qa8 OCA], [http://pdbe.org/6qa8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qa8 RCSB], [http://www.ebi.ac.uk/pdbsum/6qa8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qa8 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: Kyriakis, E]] | [[Category: Kyriakis, E]] | ||
| - | [[Category: | + | [[Category: Leonidas, D D]] |
| - | [[Category: Skamnaki, V | + | [[Category: Skamnaki, V T]] |
| - | [[Category: | + | [[Category: Stravodimos, G A]] |
| + | [[Category: Transferase]] | ||
Revision as of 07:03, 26 June 2019
Glycogen Phosphorylase b in complex with 28
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