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5l1d
From Proteopedia
(Difference between revisions)
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| - | ''' | + | {{Large structure}} |
| - | + | ==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]] 10.50Å' scene=''> | |
| - | + | == 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> | |
| - | + | </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> | |
| - | + | <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> | |
| - | [[Category: | + | <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> | ||
| + | {{Large structure}} | ||
| + | == 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
| + | [[Category: Dhindwal, S]] | ||
| + | [[Category: Lobo, J J]] | ||
| + | [[Category: Samso, M]] | ||
| + | [[Category: Calcium release channel]] | ||
| + | [[Category: Ryanodine receptor]] | ||
| + | [[Category: Transport protein-isomerase complex]] | ||
Revision as of 13:53, 24 May 2017
Warning: this is a large structure, and loading might take a long time or not happen at all.
Structure of rabbit RyR2 in complex with FKBP12.6 in a closed state (conformation C1)
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