4z5x: Difference between revisions
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''' | ==Glycogen phosphorylase in complex with gallic acid== | ||
<StructureSection load='4z5x' size='340' side='right' caption='[[4z5x]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4z5x]] 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=4Z5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z5X FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDE:3,4,5-TRIHYDROXYBENZOIC+ACID'>GDE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yua|4yua]]</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> | ||
[[Category: Kantsadi, L | <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=4z5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z5x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4z5x RCSB], [http://www.ebi.ac.uk/pdbsum/4z5x PDBsum]</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: Oryctolagus cuniculus]] | |||
[[Category: Phosphorylase]] | |||
[[Category: Chatzileontiadou, S M.D]] | |||
[[Category: Kantsadi, L A]] | |||
[[Category: Kyriakis, E]] | [[Category: Kyriakis, E]] | ||
[[Category: Leonidas, D | [[Category: Leonidas, D D]] | ||
[[Category: Stravodimos, A | [[Category: Stravodimos, A G]] | ||
[[Category: | [[Category: Alpha and beta protein]] | ||
[[Category: Transferase]] | |||
Revision as of 15:26, 13 May 2015
Glycogen phosphorylase in complex with gallic acidGlycogen phosphorylase in complex with gallic acid
Structural highlights
Function[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. |
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