2igw: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2igw.jpg|left|200px]]<br /><applet load="2igw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2igw, resolution 1.78&Aring;" />
'''CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO'''<br />


==About this Structure==
==CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO==
2IGW 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=GLY:'>GLY</scene> and <scene name='pdbligand=PRO:'>PRO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2IGW OCA].  
<StructureSection load='2igw' size='340' side='right'caption='[[2igw]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2igw]] 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=2IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGW 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]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=2igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igw OCA], [https://pdbe.org/2igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igw RCSB], [https://www.ebi.ac.uk/pdbsum/2igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igw 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/2igw_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=2igw 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: GLY]]
[[Category: PRO]]
[[Category: isomerase]]
[[Category: rotamase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:36 2008''

Latest revision as of 13:10, 30 August 2023

CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PROCYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO

Structural highlights

2igw 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 1.78Å
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

2igw, resolution 1.78Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2igw&oldid=3851755"