2cyh: Difference between revisions

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[[Image:2cyh.png|left|200px]]


{{STRUCTURE_2cyh|  PDB=2cyh  |  SCENE=  }}
==CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO==
 
<StructureSection load='2cyh' size='340' side='right'caption='[[2cyh]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
===CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2cyh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cyh 1cyh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYH FirstGlance]. <br>
{{ABSTRACT_PUBMED_8652512}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyh OCA], [https://pdbe.org/2cyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyh RCSB], [https://www.ebi.ac.uk/pdbsum/2cyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyh ProSAT]</span></td></tr>
[[2cyh]] is a 1 chain structure of [[Cyclophilin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1cyh 1cyh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYH OCA].  
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cy/2cyh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cyh ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Cyclophilin|Cyclophilin]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
<ref group="xtra">PMID:008652512</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Ke, H.]]
[[Category: Ke H]]
[[Category: Zhao, Y.]]
[[Category: Zhao Y]]
[[Category: Binding protein for cyclosporin some]]
[[Category: Cyclophilin]]
[[Category: Isomerase]]

Latest revision as of 12:18, 14 February 2024

CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PROCYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO

Structural highlights

2cyh is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1cyh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.64Å
Ligands:,
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2cyh, resolution 1.64Å

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