2qn9
From Proteopedia
(Difference between revisions)
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<StructureSection load='2qn9' size='340' side='right'caption='[[2qn9]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2qn9' size='340' side='right'caption='[[2qn9]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qn9]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qn9]] 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=2QN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN9 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=NBX:N-{[(4-AMINOPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>NBX</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=NBX:N-{[(4-AMINOPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>NBX</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qlm|2qlm]], [[2qln|2qln]], [[2qn3|2qn3]], [[2qn7|2qn7]], [[2qn8|2qn8]], [[2qnb|2qnb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qlm|2qlm]], [[2qln|2qln]], [[2qn3|2qn3]], [[2qn7|2qn7]], [[2qn8|2qn8]], [[2qnb|2qnb]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn9 OCA], [https://pdbe.org/2qn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn9 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn9 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]] | ||
Revision as of 07:44, 16 March 2022
Glycogen Phosphorylase in complex with N-4-aminobenzoyl-N'-beta-D-glucopyranosyl urea
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Categories: Large Structures | Oryctolagus cuniculus | Phosphorylase | Alexacou, K M | Chrysina, E D | Leonidas, D D | Oikonomakos, N G | Tiraidis, C | Zographos, S E | Allosteric enzyme | Carbohydrate metabolism | Glycogen metabolism | Glycogenolysis | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Pyridoxal phosphate | Transferase | Type 2 diabetes
