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.

4ctn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='4ctn' size='340' side='right'caption='[[4ctn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4ctn' size='340' side='right'caption='[[4ctn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4ctn]] 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=4CTN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CTN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4ctn]] 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=4CTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CTN 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=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=M8P:N-[(2Z,5R,7R,8S,9S,10R)-8,9,10-TRIHYDROXY-7-(HYDROXYMETHYL)-4-OXO-6-OXA-1-THIA-3-AZASPIRO[4.5]DEC-2-YLIDENE]NAPHTHALENE-2-CARBOXAMIDE'>M8P</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+
</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=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene>, <scene name='pdbligand=M8P:N-[(2Z,5R,7R,8S,9S,10R)-8,9,10-TRIHYDROXY-7-(HYDROXYMETHYL)-4-OXO-6-OXA-1-THIA-3-AZASPIRO[4.5]DEC-2-YLIDENE]NAPHTHALENE-2-CARBOXAMIDE'>M8P</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">[[4ctm|4ctm]], [[4cto|4cto]]</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=4ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ctn OCA], [https://pdbe.org/4ctn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ctn RCSB], [https://www.ebi.ac.uk/pdbsum/4ctn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ctn 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ctn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ctn OCA], [http://pdbe.org/4ctn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ctn RCSB], [http://www.ebi.ac.uk/pdbsum/4ctn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ctn 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 22: Line 20:
==See Also==
==See Also==
-
*[[Glycogen Phosphorylase|Glycogen Phosphorylase]]
+
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 29: Line 27:
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Phosphorylase]]
+
[[Category: Alexacou KM]]
-
[[Category: Alexacou, K M]]
+
[[Category: Chrysina ED]]
-
[[Category: Chrysina, E D]]
+
[[Category: Leonidas DD]]
-
[[Category: Leonidas, D D]]
+
[[Category: Papakonstantinou M]]
-
[[Category: Papakonstantinou, M]]
+
[[Category: Zographos SE]]
-
[[Category: Zographos, S E]]
+
-
[[Category: Inhibitor]]
+
-
[[Category: Structure-based drug design]]
+
-
[[Category: Transferase]]
+
-
[[Category: Type 2 diabetes]]
+

Revision as of 07:32, 14 September 2022

Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods

PDB ID 4ctn

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/4ctn"
Personal tools