+Open data
-Basic information
Entry | Database: PDB / ID: 1us7 | ||||||
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Title | Complex of Hsp90 and P50 | ||||||
Components |
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Keywords | CHAPERONE / CHAPERONE CO-CHAPERONE REGULATION / ATP-BINDING / HEAT SHOCK | ||||||
Function / homology | Function and homology information regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / The NLRP3 inflammasome / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / positive regulation of mitophagy in response to mitochondrial depolarization ...regulation of type II interferon-mediated signaling pathway / HSP90-CDC37 chaperone complex / The NLRP3 inflammasome / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / positive regulation of mitophagy in response to mitochondrial depolarization / HSF1 activation / response to oxygen levels / protein targeting to mitochondrion / protein kinase regulator activity / protein folding chaperone complex / box C/D snoRNP assembly / regulation of telomere maintenance / response to osmotic stress / 'de novo' protein folding / post-transcriptional regulation of gene expression / regulation of cyclin-dependent protein serine/threonine kinase activity / 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 type I interferon-mediated signaling pathway / protein maturation / proteasome assembly / protein targeting / RHOBTB2 GTPase cycle / Signaling by ERBB2 / Neutrophil degranulation / heat shock protein binding / positive regulation of telomere maintenance via telomerase / Constitutive Signaling by Overexpressed ERBB2 / ATP-dependent protein folding chaperone / 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 / disordered domain specific binding / unfolded protein binding / protein folding / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / cellular response to heat / protein-folding chaperone binding / protein refolding / scaffold protein binding / protein stabilization / protein kinase binding / perinuclear region of cytoplasm / ATP hydrolysis activity / protein-containing complex / extracellular exosome / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Roe, S.M. / Ali, M.M.U. / Pearl, L.H. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2004 Title: The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50(Cdc37) Authors: Roe, S.M. / Ali, M.M.U. / Meyer, P. / Vaughan, C.K. / Panaretou, B. / Piper, P.W. / Prodromou, C. / Pearl, L.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1us7.cif.gz | 100.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1us7.ent.gz | 76.2 KB | Display | PDB format |
PDBx/mmJSON format | 1us7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1us7_validation.pdf.gz | 438 KB | Display | wwPDB validaton report |
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Full document | 1us7_full_validation.pdf.gz | 447 KB | Display | |
Data in XML | 1us7_validation.xml.gz | 18.8 KB | Display | |
Data in CIF | 1us7_validation.cif.gz | 26.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/us/1us7 ftp://data.pdbj.org/pub/pdb/validation_reports/us/1us7 | HTTPS FTP |
-Related structure data
Related structure data | 1amwS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 24208.582 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-214 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P02829 |
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#2: Protein | Mass: 30869.100 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN, RESIDUES 125-378 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q16543 |
#3: Water | ChemComp-HOH / |
Compound details | FUNCTION: HSP82 IS AN ESSENTIAL PROTEIN THAT IS REQUIRED BY CELLS IN HIGHER CONCENTRATIONS FOR ...FUNCTION: HSP82 IS AN ESSENTIAL PROTEIN THAT IS REQUIRED BY CELLS IN HIGHER CONCENTRAT |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.6 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 6 Details: CRYSTALS OF THE COMPLEX WERE GROWN FROM A MIXTURE OF N-HSP90 AND C-P50 AT A FINAL CONCENTRATION OF 0.5MM AND 0.4MM RESPECTIVELY, IN A SOLUTION CONTAINING 12% POLYETHYLENE GLYCOL 4000, 16% ...Details: CRYSTALS OF THE COMPLEX WERE GROWN FROM A MIXTURE OF N-HSP90 AND C-P50 AT A FINAL CONCENTRATION OF 0.5MM AND 0.4MM RESPECTIVELY, IN A SOLUTION CONTAINING 12% POLYETHYLENE GLYCOL 4000, 16% ISOPROPANOL AND 100MM SODIUM CITRATE, PH 6.0. CRYSTAL DROPS WERE SET UP USING THE HANGING-DROP VAPOUR DIFFUSION METHOD, INITIALLY AT 4 DEGREES C FOR 48 HOURS AND THEN TRANSFERRED TO 14 DEGREES C. | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9202 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jun 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9202 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→36.3 Å / Num. obs: 26462 / % possible obs: 97.1 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.063 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.404 / Mean I/σ(I) obs: 1.9 / % possible all: 96.9 |
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 96.4 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.063 |
Reflection shell | *PLUS % possible obs: 96.4 % / Rmerge(I) obs: 0.284 / Mean I/σ(I) obs: 4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1AMW Resolution: 2.3→72.55 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.927 / SU B: 4.996 / SU ML: 0.123 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.239 / ESU R Free: 0.211 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.46 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→72.55 Å
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Refine LS restraints |
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