6l2b: Difference between revisions

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<StructureSection load='6l2b' size='340' side='right'caption='[[6l2b]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='6l2b' size='340' side='right'caption='[[6l2b]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6l2b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L2B FirstGlance]. <br>
<table><tr><td colspan='2'>[[6l2b]] is a 1 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=6L2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L2B 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</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=6l2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2b OCA], [http://pdbe.org/6l2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l2b RCSB], [http://www.ebi.ac.uk/pdbsum/6l2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2b ProSAT]</span></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=6l2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2b OCA], [https://pdbe.org/6l2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l2b RCSB], [https://www.ebi.ac.uk/pdbsum/6l2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2b 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]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail.


Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.,Venugopal V, Sen B, Datta AK, Banerjee R Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):60-4. Epub 2007 Jan 17. PMID:17277440<ref>PMID:17277440</ref>
==See Also==
 
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
</div>
<div class="pdbe-citations 6l2b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Leishmania donovani]]
[[Category: Banerjee, R]]
[[Category: Banerjee R]]
[[Category: Biswas, G]]
[[Category: Biswas G]]
[[Category: Datta, A K]]
[[Category: Datta AK]]
[[Category: Ghosh, S]]
[[Category: Ghosh S]]
[[Category: Cyclophilin]]
[[Category: Isomerase]]
[[Category: Peptidyl prolyl isomerase]]

Latest revision as of 13:50, 22 November 2023

Crystal structure of cyclophilin mutant I164M from Leishmania donovani at 2.65 angstrom resolutionCrystal structure of cyclophilin mutant I164M from Leishmania donovani at 2.65 angstrom resolution

Structural highlights

6l2b is a 1 chain structure with sequence from Leishmania donovani. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

6l2b, resolution 2.65Å

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