3o5q: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO==
==Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO==
<StructureSection load='3o5q' size='340' side='right' caption='[[3o5q]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
<StructureSection load='3o5q' size='340' side='right'caption='[[3o5q]], [[Resolution|resolution]] 0.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o5q]] is a 1 chain structure with 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=3O5Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O5Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o5q]] is a 1 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=3O5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5Q FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene><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]] 0.96&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o5d|3o5d]], [[3o5e|3o5e]], [[3o5f|3o5f]], [[3o5g|3o5g]], [[3o5i|3o5i]], [[3o5j|3o5j]], [[3o5k|3o5k]], [[3o5l|3o5l]], [[3o5m|3o5m]], [[3o5o|3o5o]], [[3o5p|3o5p]], [[3o5r|3o5r]], [[1kt0|1kt0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AIG6, FKBP5, FKBP51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3o5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5q OCA], [https://pdbe.org/3o5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5q RCSB], [https://www.ebi.ac.uk/pdbsum/3o5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5q ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o5q RCSB], [http://www.ebi.ac.uk/pdbsum/3o5q PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/FKBP5_HUMAN FKBP5_HUMAN] Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 15: Line 16:
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.,Bracher A, Kozany C, Thost AK, Hausch F Acta Crystallogr D Biol Crystallogr. 2011 Jun;67(Pt 6):549-59. Epub 2011 May 17. PMID:21636895<ref>PMID:21636895</ref>
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.,Bracher A, Kozany C, Thost AK, Hausch F Acta Crystallogr D Biol Crystallogr. 2011 Jun;67(Pt 6):549-59. Epub 2011 May 17. PMID:21636895<ref>PMID:21636895</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3o5q" style="background-color:#fffaf0;"></div>
==See Also==
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 22: Line 27:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Bracher, A.]]
[[Category: Bracher A]]
[[Category: Hausch, F.]]
[[Category: Hausch F]]
[[Category: Kozany, C.]]
[[Category: Kozany C]]
[[Category: Thost, A K.]]
[[Category: Thost A-K]]
[[Category: Fk-506 binding domain]]
[[Category: Hsp90 cochaperone]]
[[Category: Immunophiline]]
[[Category: Isomerase]]
[[Category: Peptidyl-prolyl isomerase]]