This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1wv0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:50, 9 May 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wv0]] 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=1WV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WV0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wv0]] 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=1WV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WV0 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BN4:4-[4-({[(2,4-DICHLOROBENZOYL)AMINO]CARBONYL}AMINO)-2,3-DIMETHYLPHENOXY]BUTANOIC+ACID'>BN4</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]] 2.26&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3amv|3amv]], [[1wut|1wut]], [[1wvy|1wvy]], [[1wv1|1wv1]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BN4:4-[4-({[(2,4-DICHLOROBENZOYL)AMINO]CARBONYL}AMINO)-2,3-DIMETHYLPHENOXY]BUTANOIC+ACID'>BN4</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'>[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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wv0 OCA], [https://pdbe.org/1wv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wv0 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=1wv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wv0 OCA], [https://pdbe.org/1wv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1wv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wv0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.
+
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 39: Line 38:
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Phosphorylase]]
+
[[Category: Chrysina ED]]
-
[[Category: Chrysina, E D]]
+
[[Category: Defossa E]]
-
[[Category: Defossa, E]]
+
[[Category: Klabunde T]]
-
[[Category: Klabunde, T]]
+
[[Category: Kosmopoulou MN]]
-
[[Category: Kosmopoulou, M N]]
+
[[Category: Leonidas DD]]
-
[[Category: Leonidas, D D]]
+
[[Category: Oikonomakos NG]]
-
[[Category: Oikonomakos, N G]]
+
[[Category: Wendt KU]]
-
[[Category: Wendt, K U]]
+
-
[[Category: Glycogenolysis]]
+
-
[[Category: Transferase]]
+
-
[[Category: Type 2 diabetes]]
+

Current revision

Crystallographic studies on acyl ureas, a new class of inhibitors of glycogen phosphorylase. Broad specificity of the allosteric site

PDB ID 1wv0

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/1wv0"
Personal tools