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[[Image:2igv.jpg|left|200px]]<br /><applet load="2igv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2igv, resolution 1.67&Aring;" />
'''CYCLOPHILIN 3 Complexed with DIPEPTIDE SER-PRO'''<br />


==About this Structure==
==CYCLOPHILIN 3 Complexed with DIPEPTIDE SER-PRO==
2IGV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=SER:'>SER</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGV OCA].  
<StructureSection load='2igv' size='340' side='right'caption='[[2igv]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2igv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SER:SERINE'>SER</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=2igv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igv OCA], [https://pdbe.org/2igv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igv RCSB], [https://www.ebi.ac.uk/pdbsum/2igv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYP3_CAEEL CYP3_CAEEL] 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/ig/2igv_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=2igv ConSurf].
<div style="clear:both"></div>


==Reference==
==See Also==
Experimental determination of van der waals energies in a biological system., Wear MA, Kan D, Rabu A, Walkinshaw MD, Angew Chem Int Ed Engl. 2007;46(34):6453-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17654646 17654646]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Caenorhabditis elegans]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Kan D]]
[[Category: Kan, D.]]
[[Category: SER]]
[[Category: isomerase]]
[[Category: rotamase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:38 2008''

Latest revision as of 12:03, 21 February 2024

CYCLOPHILIN 3 Complexed with DIPEPTIDE SER-PROCYCLOPHILIN 3 Complexed with DIPEPTIDE SER-PRO

Structural highlights

2igv is a 1 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.67Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYP3_CAEEL 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

2igv, resolution 1.67Å

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