2n0t
From Proteopedia
(Difference between revisions)
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+ | {{Large structure}} | ||
==Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution== | ==Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution== | ||
<StructureSection load='2n0t' size='340' side='right' caption='[[2n0t]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | <StructureSection load='2n0t' size='340' side='right' caption='[[2n0t]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2n0t]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N0T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n0t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N0T FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mzu|2mzu]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mzu|2mzu]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([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='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=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [http://pdbe.org/2n0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [http://www.ebi.ac.uk/pdbsum/2n0t 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=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [http://pdbe.org/2n0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [http://www.ebi.ac.uk/pdbsum/2n0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0t ProSAT]</span></td></tr> |
</table> | </table> | ||
{{Large structure}} | {{Large structure}} | ||
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</div> | </div> | ||
<div class="pdbe-citations 2n0t" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2n0t" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Cyclophilin|Cyclophilin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Bibow, S]] | [[Category: Bibow, S]] |
Revision as of 17:04, 15 August 2018
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Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution
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Categories: Human | Peptidylprolyl isomerase | Bibow, S | Chi, C N | Guntert, P | Orts, J | Riek, R | Strotz, D | Voegeli, B | Isomerase