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Yorodumi- PDB-3hsc: THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K HEAT-... -
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Basic information
| Entry | Database: PDB / ID: 3hsc | |||||||||
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| Title | THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K HEAT-SHOCK COGNATE PROTEIN | |||||||||
Components | HEAT-SHOCK COGNATE 7OKD PROTEIN | |||||||||
Keywords | HYDROLASE (ACTING ON ACID ANHYDRIDES) | |||||||||
| Function / homology | Function and homology informationRegulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle uncoating / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / protein targeting to lysosome involved in chaperone-mediated autophagy ...Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle uncoating / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / protein targeting to lysosome involved in chaperone-mediated autophagy / AUF1 (hnRNP D0) binds and destabilizes mRNA / clathrin coat disassembly / Clathrin-mediated endocytosis / Neutrophil degranulation / non-chaperonin molecular chaperone ATPase / : / Prp19 complex / heat shock protein binding / protein folding chaperone / RNA splicing / spliceosomal complex / ATP-dependent protein folding chaperone / mRNA processing / melanosome / presynapse / protein refolding / protein-macromolecule adaptor activity / ribonucleoprotein complex / lysosomal membrane / negative regulation of DNA-templated transcription / nucleolus / ATP hydrolysis activity / ATP binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / Resolution: 1.93 Å | |||||||||
Authors | Flaherty, K.M. / Deluca-Flaherty, C.R. / Mckay, D.B. | |||||||||
Citation | Journal: Nature / Year: 1990Title: Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Authors: Flaherty, K.M. / DeLuca-Flaherty, C. / McKay, D.B. #1: Journal: J.Biol.Chem. / Year: 1995Title: How Potassium Affects the Activity of the Molecular Chaperone Hsc70 II. Potassium Binds Specifically in the ATPase Active Site Authors: Wilbanks, S.M. / Mckay, D.B. #2: Journal: J.Biol.Chem. / Year: 1995Title: How Potassium Affects the Activity of the Molecular Chaperone Hsc70 I. Potassium is Required for Optimal ATPase Activity Authors: O'Brien, M.C. / Mckay, D.B. #3: Journal: J.Biol.Chem. / Year: 1994Title: Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein ATP Hydrolytic Activity, II. Structure of the Active Site with Adp or ATP Bound to Wild Type and Mutant ATPase Fragment Authors: Flaherty, K.M. / Wilbanks, S.M. / Deluca-Flaherty, C. / Mckay, D.B. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3hsc.cif.gz | 91.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3hsc.ent.gz | 68.2 KB | Display | PDB format |
| PDBx/mmJSON format | 3hsc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3hsc_validation.pdf.gz | 461.4 KB | Display | wwPDB validaton report |
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| Full document | 3hsc_full_validation.pdf.gz | 464.8 KB | Display | |
| Data in XML | 3hsc_validation.xml.gz | 9.3 KB | Display | |
| Data in CIF | 3hsc_validation.cif.gz | 14.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hs/3hsc ftp://data.pdbj.org/pub/pdb/validation_reports/hs/3hsc | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
-Protein , 1 types, 1 molecules A
| #1: Protein | Mass: 42513.035 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Non-polymers , 5 types, 184 molecules 








| #2: Chemical | ChemComp-MG / | ||||
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| #3: Chemical | ChemComp-PO4 / | ||||
| #4: Chemical | | #5: Chemical | ChemComp-ADP / | #6: Water | ChemComp-HOH / | |
-Details
| Nonpolymer details | SODIUM IONS HAVE BEEN IDENTIFIED BY ANALOGY TO POTASSIUM IONS LOCATED IN A HOMOLOGOUS STRUCTURE, ...SODIUM IONS HAVE BEEN IDENTIFIED |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.77 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / PH range low: 10 / PH range high: 6 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | Resolution: 1.8→44.63 Å / Num. obs: 22948 / % possible obs: 64 % / Observed criterion σ(F): 2 |
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Processing
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| Refinement | Resolution: 1.93→6 Å / σ(F): 2
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| Refinement step | Cycle: LAST / Resolution: 1.93→6 Å
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| Refine LS restraints |
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| Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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