2c4m
From Proteopedia
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==Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.== | ==Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.== | ||
| - | <StructureSection load='2c4m' size='340' side='right' caption='[[2c4m]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='2c4m' size='340' side='right'caption='[[2c4m]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2c4m]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2c4m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_callunae Corynebacterium callunae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C4M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=2c4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c4m OCA], [https://pdbe.org/2c4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c4m RCSB], [https://www.ebi.ac.uk/pdbsum/2c4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c4m ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/Q8KQ56_9CORY Q8KQ56_9CORY] 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.[RuleBase:RU000587] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c4m ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c4m ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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| + | ==See Also== | ||
| + | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Corynebacterium callunae]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Nidetzky | + | [[Category: Nidetzky B]] |
| - | [[Category: Purvis | + | [[Category: Purvis A]] |
| - | [[Category: Watson | + | [[Category: Watson K]] |
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Current revision
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.
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