5t15
From Proteopedia
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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''' | ||
| - | + | ==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]] 3.60Å' scene=''> | |
| - | + | == 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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | |
| - | [[Category: | + | <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]] | ||
Current revision
Structural basis for gating and activation of RyR1 (30 uM Ca2+ dataset, all particles)
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