3bd8
From Proteopedia
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<StructureSection load='3bd8' size='340' side='right'caption='[[3bd8]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3bd8' size='340' side='right'caption='[[3bd8]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3bd8]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3bd8]] 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=3BD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BD8 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C3B:4-AMINO-1-BETA-D-GLUCOPYRANOSYLPYRIMIDIN-2(1H)-ONE'>C3B</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=3bd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd8 OCA], [https://pdbe.org/3bd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bd8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd8 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
- | + | [[Category: Chrysina ED]] | |
- | [[Category: Chrysina | + | [[Category: Hadjiloi T]] |
- | [[Category: Hadjiloi | + | [[Category: Hayes JM]] |
- | [[Category: Hayes | + | [[Category: Oikonomakos NG]] |
- | [[Category: Oikonomakos | + | [[Category: Sovantzis DA]] |
- | [[Category: Sovantzis | + | [[Category: Zographos SE]] |
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Current revision
Glucogen Phosphorylase complex with 1(-D-glucopyranosyl) cytosine
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