5taw: Difference between revisions

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 <SX load='5taw' size='340' side='right' viewer='molstar' caption='[[5taw]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5taw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=5TAW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TAW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5taw]] 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=5TAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TAW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 4.4&#8491;</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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t15|5t15]], [[5t9m|5t9m]], [[5t9n|5t9n]], [[5t9r|5t9r]], [[5t9s|5t9s]], [[5t9v|5t9v]], [[5ta3|5ta3]], [[5tal|5tal]], [[5tam|5tam]], [[5tan|5tan]], [[5taq|5taq]], [[5tap|5tap]], [[5tas|5tas]], [[5tat|5tat]], [[5tau|5tau]], [[5tav|5tav]], [[5tax|5tax]], [[5tay|5tay]], [[5taz|5taz]], [[5tb0|5tb0]], [[5tb1|5tb1]], [[5tb2|5tb2]], [[5tb3|5tb3]], [[5tb4|5tb4]]</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=5taw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5taw OCA], [https://pdbe.org/5taw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5taw RCSB], [https://www.ebi.ac.uk/pdbsum/5taw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5taw ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP1B, FKBP12.6, FKBP1L, FKBP9, OTK4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5taw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5taw OCA], [http://pdbe.org/5taw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5taw RCSB], [http://www.ebi.ac.uk/pdbsum/5taw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5taw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RYR1_RABIT RYR1_RABIT]] Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).<ref>PMID:10388749</ref> <ref>PMID:22036948</ref>  [[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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 5taw" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ryanodine receptor 3D structures|Ryanodine receptor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Clarke OB]]
-[[Category: Clarke, O B]]
+[[Category: Frank J]]
-[[Category: Frank, J]]
+[[Category: Hendrickson WA]]
-[[Category: Georges, A des]]
+[[Category: Marks AR]]
-[[Category: Hendrickson, W A]]
+[[Category: Zalk R]]
-[[Category: Marks, A R]]
+[[Category: Des Georges A]]
-[[Category: Zalk, R]]
-[[Category: Ca2+]]
-[[Category: Ec coupling]]
-[[Category: Gating]]
-[[Category: Ryr]]
-[[Category: Transport protein-isomerase complex]]