4s1e: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 3: Line 3:
<StructureSection load='4s1e' size='340' side='right'caption='[[4s1e]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
<StructureSection load='4s1e' size='340' side='right'caption='[[4s1e]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4s1e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leido Leido]. 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 with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4S1E FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5661 LEIDO])</td></tr>
</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=4s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1e OCA], [https://pdbe.org/4s1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s1e RCSB], [https://www.ebi.ac.uk/pdbsum/4s1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s1e ProSAT]</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=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]  
[https://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]


==See Also==
==See Also==
*[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]]
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leido]]
[[Category: Leishmania donovani]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Banerjee R]]
[[Category: Banerjee, R]]
[[Category: Datta AK]]
[[Category: Datta, A K]]
[[Category: Roy S]]
[[Category: Roy, S]]
[[Category: Cytosol]]
[[Category: Isomerase]]

Revision as of 10:38, 15 March 2023

Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.

4s1e, resolution 2.22Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA