5t15: Difference between revisions

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New page: '''Unreleased structure''' The entry 5t15 is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 5t15 is ON HOLD
==Structural basis for gating and activation of RyR1 (30 uM Ca2+ dataset, all particles)==
 
<SX load='5t15' size='340' side='right' viewer='molstar' caption='[[5t15]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5t15]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T15 FirstGlance]. <br>
Description:  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5t15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t15 OCA], [https://pdbe.org/5t15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t15 RCSB], [https://www.ebi.ac.uk/pdbsum/5t15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t15 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FKB1B_HUMAN FKB1B_HUMAN] Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
__TOC__
</SX>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Clarke OB]]
[[Category: Frank J]]
[[Category: Hendrickson WA]]
[[Category: Marks AR]]
[[Category: Zalk R]]
[[Category: Des Georges A]]

Latest revision as of 18:34, 6 March 2024

Structural basis for gating and activation of RyR1 (30 uM Ca2+ dataset, all particles)Structural basis for gating and activation of RyR1 (30 uM Ca2+ dataset, all particles)

5t15, resolution 3.60Å

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OCA