1d6o: Difference between revisions

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-[[Image:1d6o.gif|left|200px]]
- {{Structure
+==NATIVE FKBP==
-|PDB= 1d6o |SIZE=350|CAPTION= <scene name='initialview01'>1d6o</scene>, resolution 1.85&Aring;
+<StructureSection load='1d6o' size='340' side='right'caption='[[1d6o]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1d6o]] is a 2 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=1D6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D6O FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6o OCA], [https://pdbe.org/1d6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d6o RCSB], [https://www.ebi.ac.uk/pdbsum/1d6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d6o ProSAT]</span></td></tr>
-|RELATEDENTRY=[[1d6o|1D6O]], [[1d7h|1D7H]], [[1d7i|1D7I]], [[1d7j|1D7J]]
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6o OCA], [http://www.ebi.ac.uk/pdbsum/1d6o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6o RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</ref>
+== 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/d6/1d6o_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=1d6o ConSurf].
+<div style="clear:both"></div>
-'''NATIVE FKBP'''
+==See Also==
+*[[FKBP 3D structures|FKBP 3D structures]]
+== References ==
-==Overview==
+<references/>
-A new crystal form of native FK506 binding protein (FKBP) has been obtained which has proved useful in ligand binding studies. Three different small molecule ligand complexes and the native enzyme have been determined at higher resolution than 2.0 A. Dissociation constants of the related small molecule ligands vary from 20 mM for dimethylsulphoxide to 200 microM for tetrahydrothiophene 1-oxide. Comparison of the four available crystal structures shows that the protein structures are identical to within experimental error, but there are differences in the water structure in the active site. Analysis of the calculated buried surface areas of these related ligands provides an estimated van der Waals contribution to the binding energy of -0.5 kJ/A(2) for non-polar interactions between ligand and protein.
+__TOC__
+</StructureSection>
-==About this Structure==
-D6O is a [[Single protein]] structure of sequence 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=1D6O OCA].
-==Reference==
-X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies., Burkhard P, Taylor P, Walkinshaw MD, J Mol Biol. 2000 Jan 28;295(4):953-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10656803 10656803]
 [[Category: Homo sapiens]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Burkhard P]]
-[[Category: Burkhard, P.]]
+[[Category: Taylor P]]
-[[Category: Taylor, P.]]
+[[Category: Walkinshaw MD]]
-[[Category: Walkinshaw, M D.]]
-[[Category: immunophilin]]
-[[Category: isomerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:41 2008''