5ls1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5ls1" [edit=sysop:move=sysop])
Current revision (18:44, 18 October 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5ls1 is ON HOLD until Paper Publication
+
==CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475==
 +
<StructureSection load='5ls1' size='340' side='right'caption='[[5ls1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5ls1]] 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=5LS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LS1 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]] 1.85&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=73Z:2-[(4-oxidanylidenecyclohexyl)amino]-4-(3,6,6-trimethyl-4-oxidanylidene-5,7-dihydroindol-1-yl)benzamide'>73Z</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=5ls1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ls1 OCA], [https://pdbe.org/5ls1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ls1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ls1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ls1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HS90A_HUMAN HS90A_HUMAN] Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function.<ref>PMID:15937123</ref> <ref>PMID:11274138</ref>
-
Authors: VALLEE, F., DUPUY, A.
+
==See Also==
-
 
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
-
Description: CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475
+
== References ==
-
[[Category: Unreleased Structures]]
+
<references/>
-
[[Category: Dupuy, A]]
+
__TOC__
-
[[Category: Vallee, F]]
+
</StructureSection>
 +
[[Category: Homo sapiens]]
 +
[[Category: Large Structures]]
 +
[[Category: Dupuy A]]
 +
[[Category: Vallee F]]

Current revision

CRYSTAL STRUCTURE OF HSP90 IN COMPLEX WITH SAR166475

PDB ID 5ls1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools