3mt9: Difference between revisions
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==Glycogen phosphorylase complexed with 4-nitrobenzaldehyde-4-(beta-D-glucopyranosyl)-thiosemicarbazone== | ==Glycogen phosphorylase complexed with 4-nitrobenzaldehyde-4-(beta-D-glucopyranosyl)-thiosemicarbazone== | ||
<StructureSection load='3mt9' size='340' side='right' caption='[[3mt9]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='3mt9' size='340' side='right'caption='[[3mt9]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mt9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3mt9]] 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=3MT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MT9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=18O:N-({(2E)-2-[(4-NITROPHENYL)METHYLIDENE]HYDRAZINO}CARBONOTHIOYL)-BETA-D-GLUCOPYRANOSYLAMINE'>18O</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></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=3mt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mt9 OCA], [https://pdbe.org/3mt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mt9 RCSB], [https://www.ebi.ac.uk/pdbsum/3mt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mt9 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3mt9" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Glycogen | *[[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: Alexacou K-M]] | |||
[[Category: Alexacou | |||