This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3hz1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:27, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of Hsp90 with fragments 37-D04 and 42-C03==
==Crystal structure of Hsp90 with fragments 37-D04 and 42-C03==
-
<StructureSection load='3hz1' size='340' side='right' caption='[[3hz1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+
<StructureSection load='3hz1' size='340' side='right'caption='[[3hz1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3hz1]] 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=3HZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HZ1 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3hz1]] 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=3HZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZ1 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=37D:METHYL+5-FURAN-2-YL-3-METHYL-1H-PYRAZOLE-4-CARBOXYLATE'>37D</scene>, <scene name='pdbligand=42C:N,N-DIMETHYL-7H-PURIN-6-AMINE'>42C</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hyy|3hyy]], [[3hyz|3hyz]], [[3hz5|3hz5]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=37D:METHYL+5-FURAN-2-YL-3-METHYL-1H-PYRAZOLE-4-CARBOXYLATE'>37D</scene>, <scene name='pdbligand=42C:N,N-DIMETHYL-7H-PURIN-6-AMINE'>42C</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=3hz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hz1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hz1 RCSB], [http://www.ebi.ac.uk/pdbsum/3hz1 PDBsum]</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=3hz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hz1 OCA], [https://pdbe.org/3hz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hz1 RCSB], [https://www.ebi.ac.uk/pdbsum/3hz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hz1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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>
+
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/3hz1_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hz/3hz1_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
+
</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=3hz1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
==See Also==
-
*[[Heat Shock Proteins|Heat Shock Proteins]]
+
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
Line 27: Line 28:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Barker, J]]
+
[[Category: Large Structures]]
-
[[Category: Cheng, R K.Y]]
+
[[Category: Barker J]]
-
[[Category: Felicetti, B]]
+
[[Category: Cheng RKY]]
-
[[Category: Mather, O]]
+
[[Category: Felicetti B]]
-
[[Category: Palan, S]]
+
[[Category: Mather O]]
-
[[Category: Whittaker, M]]
+
[[Category: Palan S]]
-
[[Category: Atp-binding]]
+
[[Category: Whittaker M]]
-
[[Category: Chaperone]]
+
-
[[Category: Nucleotide binding]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Stress response]]
+

Current revision

Crystal structure of Hsp90 with fragments 37-D04 and 42-C03

PDB ID 3hz1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools