+Open data
-Basic information
Entry | Database: PDB / ID: 1qqm | ||||||
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Title | D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN | ||||||
Components | D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN | ||||||
Keywords | HYDROLASE / HYDROLASE (ACTING ON ACID ANHYDRIDES) / MOLECULAR CHAPERONE / ATPASE | ||||||
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 / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport ...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 / 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 / synaptic vesicle uncoating / AUF1 (hnRNP D0) binds and destabilizes mRNA / clathrin coat disassembly / Clathrin-mediated endocytosis / Prp19 complex / presynaptic cytosol / postsynaptic cytosol / Neutrophil degranulation / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / autophagosome / protein folding chaperone / heat shock protein binding / RNA splicing / ATP-dependent protein folding chaperone / spliceosomal complex / terminal bouton / mRNA processing / melanosome / protein-macromolecule adaptor activity / protein refolding / ribonucleoprotein complex / lysosomal membrane / negative regulation of DNA-templated transcription / dendrite / nucleolus / ATP hydrolysis activity / ATP binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.9 Å | ||||||
Authors | Johnson, E.R. / Mckay, D.B. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein. Authors: Johnson, E.R. / McKay, D.B. #1: 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. #2: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qqm.cif.gz | 98.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qqm.ent.gz | 72.2 KB | Display | PDB format |
PDBx/mmJSON format | 1qqm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qq/1qqm ftp://data.pdbj.org/pub/pdb/validation_reports/qq/1qqm | HTTPS FTP |
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-Related structure data
-Links
-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: 41301.535 Da / Num. of mol.: 1 / Fragment: HSC70 ATPASE FRAGMENT / Mutation: D199S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P19120 |
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-Non-polymers , 6 types, 446 molecules
#2: Chemical | ChemComp-MG / | ||||||
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#3: Chemical | ChemComp-K / | ||||||
#4: Chemical | #5: Chemical | ChemComp-PO4 / | #6: Chemical | ChemComp-ADP / | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.53 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 9 Details: POLYETHYLENE GLYCOL 8000, POTASSIUM CHLORIDE, pH 9, VAPOR DIFFUSION, HANGING DROP, temperature 4K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Apr 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. all: 30759 / Num. obs: 30759 / % possible obs: 88.5 % / Observed criterion σ(I): -3 / Redundancy: 2.8 % / Biso Wilson estimate: 21.7 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 23 |
Reflection shell | Resolution: 1.9→2.02 Å / Redundancy: 2 % / Rmerge(I) obs: 0.089 / % possible all: 92.1 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 86567 |
Reflection shell | *PLUS % possible obs: 92.1 % / Num. unique obs: 5255 / Num. measured obs: 10470 / Mean I/σ(I) obs: 8.7 |
-Processing
Software |
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Refinement | Resolution: 1.9→40 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 475628.76 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 Stereochemistry target values: ENGH & HUBER, HENDRICKSON W.A. AND KONNERT J.H. Details: BIJVOET PAIRS WERE TREATED SEPARATELY IN REFINEMENT.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 59.86 Å2 / ksol: 0.384 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.9→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.5 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 3 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 20.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.291 / % reflection Rfree: 3.1 % / Rfactor Rwork: 0.258 / Rfactor obs: 0.258 |