3bcs: Difference between revisions

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==Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) uracil==
==Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) uracil==
<StructureSection load='3bcs' size='340' side='right' caption='[[3bcs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3bcs' size='340' side='right'caption='[[3bcs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3bcs]] 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=3BCS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BCS FirstGlance]. <br>
<table><tr><td colspan='2'>[[3bcs]] 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=3BCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BCS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CJB:1-BETA-D-GLUCOPYRANOSYLPYRIMIDINE-2,4(1H,3H)-DIONE'>CJB</scene></td></tr>
</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&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CJB:1-BETA-D-GLUCOPYRANOSYLPYRIMIDINE-2,4(1H,3H)-DIONE'>CJB</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bcr|3bcr]], [[3bcu|3bcu]], [[3bd6|3bd6]], [[3bd7|3bd7]], [[3bd8|3bd8]], [[3bda|3bda]]</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=3bcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcs OCA], [https://pdbe.org/3bcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bcs RCSB], [https://www.ebi.ac.uk/pdbsum/3bcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bcs ProSAT]</span></td></tr>
<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=3bcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcs OCA], [http://pdbe.org/3bcs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bcs RCSB], [http://www.ebi.ac.uk/pdbsum/3bcs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bcs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[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]]
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==See Also==
==See Also==
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Chrysina ED]]
[[Category: Chrysina, E D]]
[[Category: Hadjiloi T]]
[[Category: Hadjiloi, T]]
[[Category: Hayes JM]]
[[Category: Hayes, J M]]
[[Category: Oikonomakos NG]]
[[Category: Oikonomakos, N G]]
[[Category: Sovantzis DA]]
[[Category: Sovantzis, D A]]
[[Category: Zographos SE]]
[[Category: Zographos, S E]]
[[Category: Allosteric enzyme]]
[[Category: Carbohydrate metabolism]]
[[Category: Glycogen metabolism]]
[[Category: Glycogenolysis]]
[[Category: Glycosyltransferase]]
[[Category: Nucleotide-binding]]
[[Category: Phosphorylation]]
[[Category: Pyridoxal phosphate]]
[[Category: Transferase]]
[[Category: Type 2 diabetes]]

Latest revision as of 17:44, 1 November 2023

Glycogen Phosphorylase complex with 1(-D-glucopyranosyl) uracilGlycogen Phosphorylase complex with 1(-D-glucopyranosyl) uracil

Structural highlights

3bcs is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3bcs, resolution 2.00Å

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OCA
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