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- PDB-2qwp: Crystal structure of disulfide-bond-crosslinked complex of bovine... -
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Basic information
Entry | Database: PDB / ID: 2qwp | ||||||
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Title | Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2 | ||||||
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![]() | CHAPERONE / chaperone-cochaperone complex / ATP-binding / Nucleotide-binding / Nucleus / Phosphorylation / Stress response / Hydrolase / Protein phosphatase / SH3-binding | ||||||
Function / homology | ![]() regulation of clathrin coat assembly / 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 recycling / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand ...regulation of clathrin coat assembly / 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 recycling / 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 / clathrin heavy chain binding / late endosomal microautophagy / synaptic vesicle uncoating / AUF1 (hnRNP D0) binds and destabilizes mRNA / clathrin coat disassembly / Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases / Clathrin-mediated endocytosis / clathrin-dependent endocytosis / Prp19 complex / presynaptic cytosol / clathrin-coated vesicle / postsynaptic cytosol / Neutrophil degranulation / clathrin binding / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / intracellular transport / autophagosome / protein folding chaperone / dephosphorylation / heat shock protein binding / RNA splicing / protein tyrosine phosphatase activity / ATP-dependent protein folding chaperone / spliceosomal complex / terminal bouton / mRNA processing / SH3 domain binding / melanosome / presynapse / protein-macromolecule adaptor activity / protein refolding / vesicle / molecular adaptor activity / postsynaptic density / ribonucleoprotein complex / protein domain specific binding / lysosomal membrane / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / dendrite / nucleolus / ATP hydrolysis activity / ATP binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Jiang, J. / Maes, E.G. / Wang, L. / Taylor, A.B. / Hinck, A.P. / Lafer, E.M. / Sousa, R. | ||||||
![]() | ![]() Title: Structural basis of J cochaperone binding and regulation of Hsp70. Authors: Jiang, J. / Maes, E.G. / Taylor, A.B. / Wang, L. / Hinck, A.P. / Lafer, E.M. / Sousa, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 112.1 KB | Display | ![]() |
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PDB format | ![]() | 88.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 749.8 KB | Display | ![]() |
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Full document | ![]() | 753 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 18.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2qw9C ![]() 2qwlC ![]() 2qwmC ![]() 2qwnC ![]() 2qwoC ![]() 2qwqC ![]() 2qwrC 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 , 2 types, 2 molecules AB
#1: Protein | Mass: 43368.059 Da / Num. of mol.: 1 / Mutation: R171C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 10747.485 Da / Num. of mol.: 1 / Mutation: D876C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 7 types, 298 molecules ![](data/chem/img/PO4.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/ADP.gif)
![](data/chem/img/ACY.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-PO4 / | ||||||||||
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#4: Chemical | #5: Chemical | ChemComp-MG / | #6: Chemical | ChemComp-ADP / | #7: Chemical | ChemComp-ACY / | #8: Chemical | #9: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.92 % |
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Crystal grow | Temperature: 289 K / Method: microbatch under oil / pH: 8.5 Details: PEG3350, Ammonium Acetate, pH 8.5, microbatch under oil, temperature 289K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Detector | Date: Feb 3, 2007 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.75→50 Å / Num. obs: 48554 / % possible obs: 91.2 % / Redundancy: 6 % / Rmerge(I) obs: 0.08 / Χ2: 1.069 / Net I/σ(I): 10.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.892 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→40.66 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.75→1.795 Å / Total num. of bins used: 20
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