[English] 日本語
Yorodumi- PDB-1hpm: HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hpm | ||||||
---|---|---|---|---|---|---|---|
Title | HOW POTASSIUM AFFECTS THE ACTIVITY OF THE MOLECULAR CHAPERONE HSC70. II. POTASSIUM BINDS SPECIFICALLY IN THE ATPASE ACTIVE SITE | ||||||
Components | 44K ATPASE FRAGMENT (N-TERMINAL) OF 7O kD HEAT-SHOCK COGNATE PROTEIN | ||||||
Keywords | HYDROLASE (ACTING ON ACID ANHYDRIDES) | ||||||
Function / homology | Function and homology information 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 / chaperone-mediated autophagy translocation complex disassembly ...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 / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / protein targeting to lysosome involved in chaperone-mediated autophagy / late endosomal microautophagy / AUF1 (hnRNP D0) binds and destabilizes mRNA / clathrin coat disassembly / Clathrin-mediated endocytosis / Prp19 complex / presynaptic cytosol / Neutrophil degranulation / postsynaptic cytosol / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / autophagosome / protein folding chaperone / heat shock protein binding / RNA splicing / spliceosomal complex / ATP-dependent protein folding chaperone / terminal bouton / mRNA processing / melanosome / protein-macromolecule adaptor activity / protein refolding / lysosome / ribonucleoprotein complex / lysosomal membrane / negative regulation of DNA-templated transcription / dendrite / nucleolus / ATP hydrolysis activity / ATP binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | ||||||
Authors | Wilbanks, S.M. / Mckay, D.B. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1995 Title: 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. #1: Journal: J.Biol.Chem. / Year: 1995 Title: 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. #2: Journal: J.Biol.Chem. / Year: 1994 Title: Structural Basis of the 70-Kilodalton Heat Shock Cognate Protein ATP Hydrolytic Activity Authors: Flaherty, K.M. / Wilbanks, S.M. / Deluca-Flaherty, C. / Mckay, D.B. #3: Journal: Nature / Year: 1990 Title: Three-Dimensional Structure of the ATPase Fragment of a 70K Heat-Shock Cognate Protein Authors: Flaherty, K.M. / Deluca-Flaherty, C. / Mckay, D.B. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1hpm.cif.gz | 97.8 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1hpm.ent.gz | 71.5 KB | Display | PDB format |
PDBx/mmJSON format | 1hpm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hp/1hpm ftp://data.pdbj.org/pub/pdb/validation_reports/hp/1hpm | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: CIS PROLINE - PRO 5 |
-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.) Bos taurus (cattle) / Organ: BRAIN / Production host: Escherichia coli (E. coli) / References: UniProt: P19120, EC: 3.6.1.3 |
---|
-Non-polymers , 6 types, 436 molecules
#2: Chemical | ChemComp-MG / | ||||||
---|---|---|---|---|---|---|---|
#3: Chemical | ChemComp-PO4 / | ||||||
#4: Chemical | #5: Chemical | #6: Chemical | ChemComp-ADP / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
---|
-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.6 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6 / Method: vapor diffusion, hanging dropDetails: DeLuca-Flaherty, C., (1988) J. Mol. Biol., 200, 749. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.7→6 Å / Num. obs: 38150 / % possible obs: 82.2 % |
Reflection | *PLUS Num. obs: 39253 / Observed criterion σ(F): 2 / Num. measured all: 174376 / Rmerge(I) obs: 0.054 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor Rwork: 0.205 / Rfactor obs: 0.205 / Highest resolution: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 6 Å / Num. reflection obs: 38150 / σ(I): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |