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.
1cwc
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1cwc' size='340' side='right'caption='[[1cwc]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='1cwc' size='340' side='right'caption='[[1cwc]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1cwc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CWC FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MNL:4,N-DIMETHYLNORLEUCINE'>MNL</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></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=1cwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwc OCA], [https://pdbe.org/1cwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwc RCSB], [https://www.ebi.ac.uk/pdbsum/1cwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwc 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=1cwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwc OCA], [https://pdbe.org/1cwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cwc RCSB], [https://www.ebi.ac.uk/pdbsum/1cwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 24: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Tolypocladium inflatum]] |
| - | [[Category: Mikol | + | [[Category: Mikol V]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN
| |||||||||||

