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5kuq

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m (Protected "5kuq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5kuq is ON HOLD
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==Human cyclophilin A at 100K, Data set 4==
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<StructureSection load='5kuq' size='340' side='right' caption='[[5kuq]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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Authors: Russi, S., Gonzalez, A., Kenner, L.R., Keedy, D.A., Fraser, J.S., van den Bedem, H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kuq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KUQ FirstGlance]. <br>
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Description: Human cyclophilin A at 100K, Data set 4
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kul|5kul]], [[5kun|5kun]], [[5kuo|5kuo]], [[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]], [[5kv7|5kv7]]</td></tr>
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[[Category: Unreleased Structures]]
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<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>
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[[Category: Van Den Bedem, H]]
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<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=5kuq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kuq OCA], [http://pdbe.org/5kuq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kuq RCSB], [http://www.ebi.ac.uk/pdbsum/5kuq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kuq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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.
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__TOC__
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</StructureSection>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Bedem, H van den]]
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[[Category: Fraser, J S]]
[[Category: Gonzalez, A]]
[[Category: Gonzalez, A]]
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[[Category: Keedy, D A]]
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[[Category: Kenner, L R]]
[[Category: Russi, S]]
[[Category: Russi, S]]
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[[Category: Fraser, J.S]]
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[[Category: Conformational variation]]
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[[Category: Kenner, L.R]]
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[[Category: Isomerase]]
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[[Category: Keedy, D.A]]
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[[Category: Radiation damage]]

Revision as of 16:29, 10 August 2016

Human cyclophilin A at 100K, Data set 4

5kuq, resolution 1.70Å

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