1vbt
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1vbt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vbt, resolution 2.3Å" /> '''STRUCTURE OF CYCLOPHI...) |
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- | [[Image:1vbt.jpg|left|200px]]<br /><applet load="1vbt" size="450" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="1vbt, resolution 2.3Å" /> | ||
- | '''STRUCTURE OF CYCLOPHILIN COMPLEXED WITH SULFUR-SUBSTITUTED TETRAPEPTIDE AAPF'''<br /> | ||
- | == | + | ==Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF== |
- | + | <StructureSection load='1vbt' size='340' side='right'caption='[[1vbt]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | [[ | + | == Structural highlights == |
- | [[ | + | <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> |
- | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
- | [ | + | <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> |
- | + | <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> | ||
- | + | ==See Also== | |
+ | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Chen Y]] | ||
+ | [[Category: Fischer G]] | ||
+ | [[Category: Ke H]] | ||
+ | [[Category: Schutkowski M]] | ||
+ | [[Category: Zhao Y]] |
Current revision
Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF
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Categories: Homo sapiens | Large Structures | Chen Y | Fischer G | Ke H | Schutkowski M | Zhao Y