3t3h: Difference between revisions

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[[Image:3t3h.jpg|left|200px]]


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==Glycogen Phosphorylase b in complex with GlcIU==
The line below this paragraph, containing "STRUCTURE_3t3h", creates the "Structure Box" on the page.
<StructureSection load='3t3h' size='340' side='right'caption='[[3t3h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3t3h]] 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=3T3H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3H FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GPV:1-(BETA-D-GLUCOPYRANOSYL)-5-IODOPYRIMIDINE-2,4(1H,3H)-DIONE'>GPV</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>
{{STRUCTURE_3t3h|  PDB=3t3h  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3h OCA], [https://pdbe.org/3t3h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3h RCSB], [https://www.ebi.ac.uk/pdbsum/3t3h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3h 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.


===Glycogen Phosphorylase b in complex with GlcIU===
==See Also==
 
*[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]]
 
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</StructureSection>
The line below this paragraph, {{ABSTRACT_PUBMED_22267166}}, adds the Publication Abstract to the page
[[Category: Large Structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 22267166 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22267166}}
 
==About this Structure==
[[3t3h]] 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=3T3H OCA].
 
==Reference==
<ref group="xtra">PMID:022267166</ref><references group="xtra"/>
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Phosphorylase]]
[[Category: Kantsadi AL]]
[[Category: Kantsadi, A L.]]
[[Category: Leonidas DD]]
[[Category: Leonidas, D D.]]
[[Category: Skamnaki VT]]
[[Category: Skamnaki, V T.]]
[[Category: A+b protein]]
[[Category: Muscle]]
[[Category: Transferase]]
[[Category: Transferase-transferase inhibitor complex]]

Latest revision as of 16:16, 14 March 2024

Glycogen Phosphorylase b in complex with GlcIUGlycogen Phosphorylase b in complex with GlcIU

Structural highlights

3t3h 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 2.6Å
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

3t3h, resolution 2.60Å

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