This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2haq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal Structure of Cyclophilin A from Leishmania Donovani==
==Crystal Structure of Cyclophilin A from Leishmania Donovani==
-
<StructureSection load='2haq' size='340' side='right' caption='[[2haq]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
+
<StructureSection load='2haq' size='340' side='right'caption='[[2haq]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2haq]] is a 1 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=2HAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HAQ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2haq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HAQ 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5661 LEIDO])</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'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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=2haq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haq OCA], [http://pdbe.org/2haq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2haq RCSB], [http://www.ebi.ac.uk/pdbsum/2haq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2haq 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=2haq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haq OCA], [https://pdbe.org/2haq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2haq RCSB], [https://www.ebi.ac.uk/pdbsum/2haq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2haq 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]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 29: Line 29:
</div>
</div>
<div class="pdbe-citations 2haq" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2haq" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Leido]]
[[Category: Leido]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]

Revision as of 07:35, 17 March 2021

Crystal Structure of Cyclophilin A from Leishmania Donovani

PDB ID 2haq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools