5l1d: Difference between revisions

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{{Large structure}}
 
==Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)==
==Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)==
<StructureSection load='5l1d' size='340' side='right' caption='[[5l1d]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
<SX load='5l1d' size='340' side='right' viewer='molstar' caption='[[5l1d]], [[Resolution|resolution]] 10.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5l1d]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L1D FirstGlance]. <br>
<table><tr><td colspan='2'>[[5l1d]] 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=5L1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L1D FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=5l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1d OCA], [https://pdbe.org/5l1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l1d RCSB], [https://www.ebi.ac.uk/pdbsum/5l1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1d ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l1d OCA], [http://pdbe.org/5l1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l1d RCSB], [http://www.ebi.ac.uk/pdbsum/5l1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l1d ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
== Function ==
== Function ==
[[http://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.  
[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__
__TOC__
</StructureSection>
</SX>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Dhindwal S]]
[[Category: Dhindwal, S]]
[[Category: Lobo JJ]]
[[Category: Lobo, J J]]
[[Category: Samso M]]
[[Category: Samso, M]]
[[Category: Calcium release channel]]
[[Category: Ryanodine receptor]]
[[Category: Transport protein-isomerase complex]]

Latest revision as of 15:42, 6 March 2024

Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)

5l1d, resolution 10.50Å

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