4el0

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4el0]] 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=4EL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EL0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4el0]] 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=4EL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EL0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1K:3-(BETA-D-GLUCOPYRANOSYL)-6-PROPYLFURO[2,3-D]PYRIMIDIN-2(3H)-ONE'>D1K</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1K:3-(BETA-D-GLUCOPYRANOSYL)-6-PROPYLFURO[2,3-D]PYRIMIDIN-2(3H)-ONE'>D1K</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4el0 OCA], [https://pdbe.org/4el0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4el0 RCSB], [https://www.ebi.ac.uk/pdbsum/4el0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4el0 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4el0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4el0 OCA], [https://pdbe.org/4el0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4el0 RCSB], [https://www.ebi.ac.uk/pdbsum/4el0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4el0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 08:21, 6 December 2023

Crystal structure of GPb in complex with DK16

PDB ID 4el0

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