+Open data
-Basic information
Entry | Database: PDB / ID: 2n5x | ||||||
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Title | C-terminal domain of Cdc37 cochaperone | ||||||
Components | Hsp90 co-chaperone Cdc37 | ||||||
Keywords | CHAPERONE / cdc37 / Hsp90 / kinase / co-chaperone | ||||||
Function / homology | Function and homology information regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of mitophagy in response to mitochondrial depolarization / protein kinase regulator activity / protein folding chaperone complex / post-transcriptional regulation of gene expression / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib ...regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / positive regulation of mitophagy in response to mitochondrial depolarization / protein kinase regulator activity / protein folding chaperone complex / post-transcriptional regulation of gene expression / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / regulation of cyclin-dependent protein serine/threonine kinase activity / regulation of type I interferon-mediated signaling pathway / protein targeting / RHOBTB2 GTPase cycle / Signaling by ERBB2 / heat shock protein binding / Constitutive Signaling by Overexpressed ERBB2 / Signaling by ERBB2 TMD/JMD mutants / Hsp90 protein binding / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / Regulation of necroptotic cell death / Downregulation of ERBB2 signaling / kinase binding / unfolded protein binding / protein folding / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / protein-folding chaperone binding / scaffold protein binding / protein stabilization / protein kinase binding / extracellular exosome / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Keramisanou, D. / Dudhat, A. / Pare, M. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2015 Title: The C-terminal domain of human Cdc37 studied by solution NMR. Authors: Zhang, Z. / Keramisanou, D. / Dudhat, A. / Pare, M. / Gelis, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n5x.cif.gz | 320.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n5x.ent.gz | 271.3 KB | Display | PDB format |
PDBx/mmJSON format | 2n5x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n5/2n5x ftp://data.pdbj.org/pub/pdb/validation_reports/n5/2n5x | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10197.366 Da / Num. of mol.: 1 / Fragment: C-terminal domain of Cdc37, UNP residues 288-378 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CDC37, CDC37A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q16543 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 7.5 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |