2c4m: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
Line 3: Line 3:
<StructureSection load='2c4m' size='340' side='right'caption='[[2c4m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2c4m' size='340' side='right'caption='[[2c4m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2c4m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15991 Atcc 15991]. 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>
<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" 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<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='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'>[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>
<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]  
[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]]
Line 25: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 15991]]
[[Category: Corynebacterium callunae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphorylase]]
[[Category: Nidetzky B]]
[[Category: Nidetzky, B]]
[[Category: Purvis A]]
[[Category: Purvis, A]]
[[Category: Watson K]]
[[Category: Watson, K]]
[[Category: Allosteric control]]
[[Category: Glycosyltransferase]]
[[Category: Phosphate dependence]]
[[Category: Starch degrading]]
[[Category: Transferase]]

Latest revision as of 14:05, 13 December 2023

Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control.

2c4m, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA