1vbt: Difference between revisions

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OCA

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 ==Structure of cyclophilin complexed with sulfur-substituted tetrapeptide AAPF==
-<StructureSection load='1vbt' size='340' side='right' caption='[[1vbt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1vbt' size='340' side='right'caption='[[1vbt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vbt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VBT FirstGlance]. <br>
+<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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALT:THIOALANINE'>ALT</scene>, <scene name='pdbligand=NIT:4-NITROANILINE'>NIT</scene></td></tr>
+</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>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vbt OCA], [http://pdbe.org/1vbt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vbt RCSB], [http://www.ebi.ac.uk/pdbsum/1vbt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vbt ProSAT]</span></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]]
@@ Line 20: / Line 22: @@
 ==See Also==
-*[[Cyclophilin|Cyclophilin]]
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[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: Isomerase-isomerase substrate complex]]
-[[Category: Peptidyl-prolyl isomerase]]