2qn3
From Proteopedia
(Difference between revisions)
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<StructureSection load='2qn3' size='340' side='right'caption='[[2qn3]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='2qn3' size='340' side='right'caption='[[2qn3]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2qn3]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2qn3]] 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=2QN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN3 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F55:N-{[(4-CHLOROPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>F55</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F55:N-{[(4-CHLOROPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>F55</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qlm|2qlm]], [[2qln|2qln]], [[2qn7|2qn7]], [[2qn8|2qn8]], [[2qn9|2qn9]], [[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]], [[2qn7|2qn7]], [[2qn8|2qn8]], [[2qn9|2qn9]], [[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=2qn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn3 OCA], [https://pdbe.org/2qn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn3 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-chlorobenzoyl-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 | Acetylation | Allosteric enzyme | Carbohydrate metabolism | Glycogen metabolism | Glycogenolysis | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Pyridoxal phosphate | Transferase | Type 2 diabetes
