5kv3: Difference between revisions

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'''Unreleased structure'''


The entry 5kv3 is ON HOLD
==Human cyclophilin A at 278K, Data set 5==
 
<StructureSection load='5kv3' size='340' side='right' caption='[[5kv3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
Authors: Russi, S., Gonzalez, A., Kenner, L.R., Keedy, D.A., Fraser, J.S., van den Bedem, H.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5kv3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KV3 FirstGlance]. <br>
Description: Human cyclophilin A at 278K, Data set 5
</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]], [[5kv4|5kv4]], [[5kv5|5kv5]], [[5kv6|5kv6]], [[5kv7|5kv7]]</td></tr>
[[Category: Unreleased Structures]]
<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: Van Den Bedem, H]]
<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=5kv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kv3 OCA], [http://pdbe.org/5kv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5kv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kv3 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: Fraser, J.S]]
[[Category: Conformational variation]]
[[Category: Kenner, L.R]]
[[Category: Isomerase]]
[[Category: Keedy, D.A]]
[[Category: Radiation damage]]

Revision as of 19:30, 10 August 2016

Human cyclophilin A at 278K, Data set 5Human cyclophilin A at 278K, Data set 5

Structural highlights

5kv3 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

5kv3, resolution 1.70Å

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OCA
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