We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6s4h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:14, 9 April 2025) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6s4h' size='340' side='right'caption='[[6s4h]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='6s4h' size='340' side='right'caption='[[6s4h]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6s4h]] 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=6S4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S4H FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6s4h]] 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=6S4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S4H FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=KUQ:(2~{R},3~{S},4~{R},5~{R},6~{S})-2-(hydroxymethyl)-6-(2-phenyl-1~{H}-imidazol-4-yl)oxane-3,4,5-triol'>KUQ</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]] 2.45&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=KUQ:(2~{R},3~{S},4~{R},5~{R},6~{S})-2-(hydroxymethyl)-6-(2-phenyl-1~{H}-imidazol-4-yl)oxane-3,4,5-triol'>KUQ</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=6s4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s4h OCA], [http://pdbe.org/6s4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s4h RCSB], [http://www.ebi.ac.uk/pdbsum/6s4h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s4h 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=6s4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s4h OCA], [https://pdbe.org/6s4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s4h RCSB], [https://www.ebi.ac.uk/pdbsum/6s4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s4h 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 19: Line 19:
</div>
</div>
<div class="pdbe-citations 6s4h" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6s4h" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 25: Line 28:
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Phosphorylase]]
+
[[Category: Kyriakis E]]
-
[[Category: Kyriakis, E]]
+
[[Category: Leonidas DD]]
-
[[Category: Leonidas, D D]]
+
[[Category: Papaioannou OSE]]
-
[[Category: Papaioannou, O S.E]]
+
[[Category: Skamnaki VT]]
-
[[Category: Skamnaki, V T]]
+
[[Category: Solovou TGA]]
-
[[Category: Solovou, T G.A]]
+
-
[[Category: C-beta-d-glucopyranosyl imidazole]]
+
-
[[Category: Inhibitor]]
+
-
[[Category: Transferase]]
+

Current revision

The crystal structure of glycogen phosphorylase in complex with 8

PDB ID 6s4h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6s4h"
Personal tools