5ox1: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Glycogen Phosphorylase in complex with JLH270==
==Glycogen Phosphorylase in complex with JLH270==
<StructureSection load='5ox1' size='340' side='right' caption='[[5ox1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='5ox1' size='340' side='right'caption='[[5ox1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ox1]] 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=5OX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OX1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ox1]] 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=5OX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OX1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B1K:(2~{R},3~{S},4~{R},5~{R},6~{S})-2-(hydroxymethyl)-6-[5-(4-methoxyphenyl)-1~{H}-1,2,4-triazol-3-yl]oxane-3,4,5-triol'>B1K</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</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]] 1.85&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5owy|5owy]], [[5owz|5owz]], [[5ox0|5ox0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1K:(2~{R},3~{S},4~{R},5~{R},6~{S})-2-(hydroxymethyl)-6-[5-(4-methoxyphenyl)-1~{H}-1,2,4-triazol-3-yl]oxane-3,4,5-triol'>B1K</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=5ox1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ox1 OCA], [https://pdbe.org/5ox1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ox1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ox1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ox1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ox1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ox1 OCA], [http://pdbe.org/5ox1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ox1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ox1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ox1 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 5ox1" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5ox1" style="background-color:#fffaf0;"></div>
==See Also==
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[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]]