4ca9
From Proteopedia
(Difference between revisions)
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==Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39== | ==Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39== | ||
<StructureSection load='4ca9' size='340' side='right' caption='[[4ca9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='4ca9' size='340' side='right' caption='[[4ca9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[4ca9]] is a 5 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CA9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ca9]] is a 5 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CA9 FirstGlance]. <br> | ||
</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> | </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=4ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ca9 PDBsum]</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=4ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ca9 OCA], [http://pdbe.org/4ca9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ca9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ca9 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | [[http://www.uniprot.org/uniprot/FKB39_DROME FKB39_DROME]] PPIases accelerate the folding of proteins. May function in a signal transduction cascade during early development. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4ca9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Revision as of 17:28, 9 March 2017
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Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39
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