2ff5: Difference between revisions

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[[Image:2ff5.jpg|left|200px]]


{{Structure
==Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal==
|PDB= 2ff5 |SIZE=350|CAPTION= <scene name='initialview01'>2ff5</scene>, resolution 2.03&Aring;
<StructureSection load='2ff5' size='340' side='right'caption='[[2ff5]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene> and <scene name='pdbligand=H53:2-(2,5-DIHYDROXYPHENYL)-6-(HYDROXYMETHYL)OXANE-3,4,5-TRIOL'>H53</scene>
<table><tr><td colspan='2'>[[2ff5]] 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=2FF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FF5 FirstGlance]. <br>
|ACTIVITY= [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]  
</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>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H53:2-(2,5-DIHYDROXYPHENYL)-6-(HYDROXYMETHYL)OXANE-3,4,5-TRIOL'>H53</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=2ff5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ff5 OCA], [https://pdbe.org/2ff5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ff5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ff5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ff5 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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ff/2ff5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ff5 ConSurf].
<div style="clear:both"></div>


'''Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal'''
==See Also==
 
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
2FF5 is a [[Single protein]] structure of 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=2FF5 OCA].
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Chrysina ED]]
[[Category: Single protein]]
[[Category: Kosmopoulou MN]]
[[Category: Chrysina, E D.]]
[[Category: Leonidas DD]]
[[Category: Kosmopoulou, M N.]]
[[Category: Oikonomakos NG]]
[[Category: Leonidas, D D.]]
[[Category: Oikonomakos, N G.]]
[[Category: H53]]
[[Category: PLP]]
[[Category: glycogenolysis; type 2 diabetes]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:05:23 2008''

Latest revision as of 12:26, 30 August 2023

Synthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystalSynthesis of C-D-Glycopyranosyl-Hydroquinones and-Benzoquinones. Inhibition of PTP1B. Inhibition of and binding to glycogen phosphorylase in the crystal

Structural highlights

2ff5 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2ff5, resolution 2.03Å

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