4s1e
From Proteopedia
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==Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.== | ==Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.== | ||
<StructureSection load='4s1e' size='340' side='right' caption='[[4s1e]], [[Resolution|resolution]] 2.22Å' scene=''> | <StructureSection load='4s1e' size='340' side='right' caption='[[4s1e]], [[Resolution|resolution]] 2.22Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4s1e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S1E FirstGlance]. <br> | <table><tr><td colspan='2'>[[4s1e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S1E 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=4s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4s1e RCSB], [http://www.ebi.ac.uk/pdbsum/4s1e 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=4s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1e OCA], [http://pdbe.org/4s1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s1e RCSB], [http://www.ebi.ac.uk/pdbsum/4s1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s1e ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | [[http://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | ||
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| + | ==See Also== | ||
| + | *[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 01:20, 19 January 2017
Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.
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