5ox0: Difference between revisions

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<StructureSection load='5ox0' size='340' side='right'caption='[[5ox0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='5ox0' size='340' side='right'caption='[[5ox0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ox0]] 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=5OX0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OX0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ox0]] 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=5OX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OX0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1H:(1S)-1,5-anhydro-1-(3-{4-[hydroxy(oxo)azaniumyl]phenyl}-1H-1,2,4-triazol-5-yl)-D-glucitol'>B1H</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1H:(1S)-1,5-anhydro-1-(3-{4-[hydroxy(oxo)azaniumyl]phenyl}-1H-1,2,4-triazol-5-yl)-D-glucitol'>B1H</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5owy|5owy]], [[5owz|5owz]]</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=5ox0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ox0 OCA], [https://pdbe.org/5ox0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ox0 RCSB], [https://www.ebi.ac.uk/pdbsum/5ox0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ox0 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://proteopedia.org/fgij/fg.htm?mol=5ox0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ox0 OCA], [http://pdbe.org/5ox0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ox0 RCSB], [http://www.ebi.ac.uk/pdbsum/5ox0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ox0 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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Chatzileontiadou DSM]]
[[Category: Chatzileontiadou, D S.M]]
[[Category: Kantsadi AL]]
[[Category: Kantsadi, A L]]
[[Category: Kyriakis E]]
[[Category: Kyriakis, E]]
[[Category: Leonidas DD]]
[[Category: Leonidas, D D]]
[[Category: Stravodimos GA]]
[[Category: Stravodimos, G A]]
[[Category: Transferase]]

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