5kv7
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Human cyclophilin A at 278K, Data set 9== | |
| - | + | <StructureSection load='5kv7' size='340' side='right' caption='[[5kv7]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5kv7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KV7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KV7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kul|5kul]], [[5kun|5kun]], [[5kuo|5kuo]], [[5kuq|5kuq]], [[5kur|5kur]], [[5kus|5kus]], [[5kuu|5kuu]], [[5kuv|5kuv]], [[5kuw|5kuw]], [[5kuz|5kuz]], [[5kv0|5kv0]], [[5kv1|5kv1]], [[5kv2|5kv2]], [[5kv3|5kv3]], [[5kv4|5kv4]], [[5kv5|5kv5]], [[5kv6|5kv6]]</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> |
| - | [[Category: | + | <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=5kv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kv7 OCA], [http://pdbe.org/5kv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kv7 RCSB], [http://www.ebi.ac.uk/pdbsum/5kv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kv7 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: Bedem, H van den]] | ||
| + | [[Category: Fraser, J S]] | ||
[[Category: Gonzalez, A]] | [[Category: Gonzalez, A]] | ||
| + | [[Category: Keedy, D A]] | ||
| + | [[Category: Kenner, L R]] | ||
[[Category: Russi, S]] | [[Category: Russi, S]] | ||
| - | [[Category: | + | [[Category: Conformational variation]] |
| - | [[Category: | + | [[Category: Isomerase]] |
| - | [[Category: | + | [[Category: Radiation damage]] |
Revision as of 13:59, 10 September 2016
Human cyclophilin A at 278K, Data set 9
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