3zcs: Difference between revisions

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New page: '''Unreleased structure''' The entry 3zcs is ON HOLD Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, ...
 
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'''Unreleased structure'''


The entry 3zcs is ON HOLD
==Rabbit muscle glycogen phosphorylase b in complex with N-(1-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.07 A resolution==
<StructureSection load='3zcs' size='340' side='right'caption='[[3zcs]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zcs]] 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=3ZCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZCS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAW:N-[[(2R,3R,4S,5S,6R)-6-(HYDROXYMETHYL)-3,4,5-TRIS(OXIDANYL)OXAN-2-YL]CARBAMOYL]NAPHTHALENE-1-CARBOXAMIDE'>CAW</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</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'>[https://proteopedia.org/fgij/fg.htm?mol=3zcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zcs OCA], [https://pdbe.org/3zcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zcs RCSB], [https://www.ebi.ac.uk/pdbsum/3zcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zcs ProSAT]</span></td></tr>
</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.


Authors: Chrysina, E.D., Nagy, V., Felfoldi, N., Konya, B., Telepo, K., Praly, J.P., Docsa, T., Gergely, P., Alexacou, K.M., Hayes, J.M., Konstantakaki, M., Kardakaris, R., Leonidas, D.D., Zographos, S.E., Oikonomakos, N.G., Somsak, L.
==See Also==
 
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
Description: Rabbit muscle glycogen phosphorylase b in complex with N-(1-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.07 A resolution
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Alexacou KM]]
[[Category: Chrysina ED]]
[[Category: Docsa T]]
[[Category: Felfoldi N]]
[[Category: Gergely P]]
[[Category: Hayes JM]]
[[Category: Kardakaris R]]
[[Category: Konstantakaki M]]
[[Category: Konya B]]
[[Category: Leonidas DD]]
[[Category: Nagy V]]
[[Category: Oikonomakos NG]]
[[Category: Praly JP]]
[[Category: Somsak L]]
[[Category: Telepo K]]
[[Category: Zographos SE]]

Latest revision as of 13:58, 20 December 2023

Rabbit muscle glycogen phosphorylase b in complex with N-(1-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.07 A resolutionRabbit muscle glycogen phosphorylase b in complex with N-(1-naphthoyl) -N-beta-D-glucopyranosyl urea determined at 2.07 A resolution

Structural highlights

3zcs is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.03Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

See Also

3zcs, resolution 2.03Å

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