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- PDB-1ba1: HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL MUTANT WIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ba1 | ||||||
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Title | HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL MUTANT WITH CYS 17 REPLACED BY LYS | ||||||
![]() | HEAT-SHOCK COGNATE 70KD PROTEIN | ||||||
![]() | HYDROLASE / ACTING ON ACID ANHYDRIDES / ATP-BINDING / HEAT SHOCK | ||||||
Function / homology | ![]() 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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wilbanks, S.M. / Mckay, D.B. | ||||||
![]() | ![]() Title: Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70. Authors: Wilbanks, S.M. / McKay, D.B. #1: ![]() Title: 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. #2: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.1 KB | Display | ![]() |
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PDB format | ![]() | 71.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 720.3 KB | Display | ![]() |
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Full document | ![]() | 722 KB | Display | |
Data in XML | ![]() | 20.4 KB | Display | |
Data in CIF | ![]() | 31.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ba0C ![]() 1hpmS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 42539.074 Da / Num. of mol.: 1 / Fragment: 44KD ATPASE N-TERMINAL FRAGMENT / Mutation: C17K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 447 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / | ||||
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#3: Chemical | ChemComp-NA / | ||||
#4: Chemical | #5: Chemical | ChemComp-ADP / | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.73 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 9 Details: 20% PEG-8000 1.0M NACL 50MM CHES, PH 9 1MM MGATP, pH 9.0 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Oct 1, 1995 |
Radiation | Monochromator: GRAPHITE(002) / 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. obs: 34106 / % possible obs: 99 % / Observed criterion σ(I): 3 / Redundancy: 3.2 % / Rmerge(I) obs: 1 / Rsym value: 0.056 / Net I/σ(I): 16 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 1.2 % / Rmerge(I) obs: 1 / Mean I/σ(I) obs: 12 / Rsym value: 0.133 / % possible all: 69.7 |
Reflection | *PLUS Highest resolution: 1.7 Å / Num. obs: 45230 / % possible obs: 94.7 % / Num. measured all: 138386 / Rmerge(I) obs: 0.051 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HPM Resolution: 1.7→6 Å / Rfactor Rfree error: 0.6 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Cross valid method: THROUGHOUT / σ(F): 2 / Details: SCALE ORTHORHOMBIC, LONGEST AXIS FIRST
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Refine analyze | Luzzati coordinate error obs: 0.3 Å / Luzzati d res low obs: 40 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.76 Å / Rfactor Rfree error: 0.6 / Total num. of bins used: 10
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