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.
6gjy
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cyclophilin A complexed with tri-vector ligand 5.== | |
| - | + | <StructureSection load='6gjy' size='340' side='right' caption='[[6gjy]], [[Resolution|resolution]] 1.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6gjy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GJY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GJY FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F1Z:ethyl+2-[[(4-aminophenyl)methyl-prop-2-ynyl-carbamoyl]amino]ethanoate'>F1Z</scene></td></tr> | |
| - | [[Category: | + | <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=6gjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gjy OCA], [http://pdbe.org/6gjy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gjy RCSB], [http://www.ebi.ac.uk/pdbsum/6gjy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gjy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Georgiou, C]] | [[Category: Georgiou, C]] | ||
[[Category: Michel, J]] | [[Category: Michel, J]] | ||
| - | [[Category: | + | [[Category: Simone, A De]] |
| - | [[Category: Walkinshaw, M | + | [[Category: Walkinshaw, M D]] |
| + | [[Category: Complex]] | ||
| + | [[Category: Cyclophilin]] | ||
| + | [[Category: Cypa]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Ppiase]] | ||
Revision as of 12:18, 7 November 2018
Cyclophilin A complexed with tri-vector ligand 5.
| |||||||||||
Categories: Peptidylprolyl isomerase | Georgiou, C | Michel, J | Simone, A De | Walkinshaw, M D | Complex | Cyclophilin | Cypa | Inhibitor | Isomerase | Ppiase
