3nmq: Difference between revisions

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New page: '''Unreleased structure''' The entry 3nmq is ON HOLD Authors: Arndt, J. W., Yun, T. J., Harning, E. K., Giza, K., Rabah, D., Li, P., Luchetti, D., Shi, J., Manning, A., Kehry, M. R. De...
 
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'''Unreleased structure'''


The entry 3nmq is ON HOLD
==Hsp90b N-terminal domain in complex with EC44, a pyrrolo-pyrimidine methoxypyridine inhibitor==
<StructureSection load='3nmq' size='340' side='right'caption='[[3nmq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nmq]] 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=3NMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NMQ 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7PP:5-{2-AMINO-4-CHLORO-7-[(4-METHOXY-3,5-DIMETHYLPYRIDIN-2-YL)METHYL]-7H-PYRROLO[2,3-D]PYRIMIDIN-5-YL}-2-METHYLPENT-4-YN-2-OL'>7PP</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=3nmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmq OCA], [https://pdbe.org/3nmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nmq RCSB], [https://www.ebi.ac.uk/pdbsum/3nmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nmq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HS90B_HUMAN HS90B_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:16478993</ref> <ref>PMID:19696785</ref>


Authors: Arndt, J. W., Yun, T. J., Harning, E. K., Giza, K., Rabah, D., Li, P., Luchetti, D., Shi, J., Manning, A., Kehry, M. R.
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
Description: Hsp90b N-terminal domain in complex with EC44, a pyrrolo-pyrimidine methoxypyridine inhibitor
== References ==
 
<references/>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 30 13:37:18 2010''
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arndt JW]]
[[Category: Giza K]]
[[Category: Harning EK]]
[[Category: Kehry MR]]
[[Category: Li P]]
[[Category: Luchetti D]]
[[Category: Manning A]]
[[Category: Rabah D]]
[[Category: Shi J]]
[[Category: Yun TJ]]

Latest revision as of 14:05, 13 March 2024

Hsp90b N-terminal domain in complex with EC44, a pyrrolo-pyrimidine methoxypyridine inhibitor

3nmq, resolution 2.20Å

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