1vbt: Difference between revisions

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[[Image:1vbt.png|left|200px]]


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==Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF==
The line below this paragraph, containing "STRUCTURE_1vbt", creates the "Structure Box" on the page.
<StructureSection load='1vbt' size='340' side='right'caption='[[1vbt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1vbt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VBT FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALT:THIOALANINE'>ALT</scene>, <scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene></td></tr>
{{STRUCTURE_1vbt| PDB=1vbt |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vbt OCA], [https://pdbe.org/1vbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vbt RCSB], [https://www.ebi.ac.uk/pdbsum/1vbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vbt ProSAT]</span></td></tr>
</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/vb/1vbt_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=1vbt ConSurf].
<div style="clear:both"></div>


===STRUCTURE OF CYCLOPHILIN COMPLEXED WITH SULFUR-SUBSTITUTED TETRAPEPTIDE AAPF===
==See Also==
 
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
__TOC__
==About this Structure==
</StructureSection>
1VBT is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VBT OCA].
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Chen, Y.]]
[[Category: Large Structures]]
[[Category: Fischer, G.]]
[[Category: Chen Y]]
[[Category: Ke, H.]]
[[Category: Fischer G]]
[[Category: Schutkowski, M.]]
[[Category: Ke H]]
[[Category: Zhao, Y.]]
[[Category: Schutkowski M]]
[[Category: Competitive inhibitor]]
[[Category: Zhao Y]]
[[Category: Cyclophilin some]]
[[Category: Mechanism]]
[[Category: Peptidyl-prolyl isomerase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 08:55:11 2009''

Latest revision as of 09:17, 3 April 2024

Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPFStructure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF

Structural highlights

1vbt is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
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

1vbt, resolution 2.30Å

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