1p4h
From Proteopedia
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| - | [[Image:1p4h.png|left|200px]] | ||
| - | + | ==Crystal structure of glycogen phosphorylase b in complex with C-(1-acetamido-alpha-D-glucopyranosyl) formamide== | |
| - | + | <StructureSection load='1p4h' size='340' side='right'caption='[[1p4h]], [[Resolution|resolution]] 2.06Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1p4h]] 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=1P4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P4H FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.06Å</td></tr> | |
| - | == | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR6:1-DEOXY-1-ACETYLAMINO-BETA-D-GLUCO-2-HEPTULOPYRANOSONAMIDE'>CR6</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | [[1p4h]] is a 1 chain structure with sequence from [ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1p4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4h OCA], [https://pdbe.org/1p4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p4h RCSB], [https://www.ebi.ac.uk/pdbsum/1p4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p4h ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == 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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p4/1p4h_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1p4h ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Glycogen | + | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
| - | + | [[Category: Bischler N]] | |
| - | [[Category: Bischler | + | [[Category: Chrysina ED]] |
| - | [[Category: Chrysina | + | [[Category: Gergely P]] |
| - | [[Category: Gergely | + | [[Category: Kosmopoulou MN]] |
| - | [[Category: Kosmopoulou | + | [[Category: Leonidas DD]] |
| - | [[Category: Leonidas | + | [[Category: Nagy V]] |
| - | [[Category: Nagy | + | [[Category: Oikonomakos NG]] |
| - | [[Category: Oikonomakos | + | [[Category: Praly J-P]] |
| - | [[Category: Praly | + | [[Category: Somsak L]] |
| - | [[Category: Somsak | + | [[Category: Zographos SE]] |
| - | [[Category: Zographos | + | |
| - | + | ||
Current revision
Crystal structure of glycogen phosphorylase b in complex with C-(1-acetamido-alpha-D-glucopyranosyl) formamide
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