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- PDB-1dkg: CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1dkg | ||||||
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Title | CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK | ||||||
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![]() | COMPLEX (HSP24/HSP70) / HSP70 / GRPE / MOLECULAR CHAPERONE / NUCLEOTIDE EXCHANGE FACTOR / COILED-COIL / COMPLEX (HSP24-HSP70) / COMPLEX (HSP24-HSP70) complex | ||||||
Function / homology | ![]() protein-containing complex disassembly / stress response to copper ion / adenyl-nucleotide exchange factor activity / sigma factor antagonist activity / chaperone cofactor-dependent protein refolding / protein unfolding / cellular response to unfolded protein / protein folding chaperone / inclusion body / heat shock protein binding ...protein-containing complex disassembly / stress response to copper ion / adenyl-nucleotide exchange factor activity / sigma factor antagonist activity / chaperone cofactor-dependent protein refolding / protein unfolding / cellular response to unfolded protein / protein folding chaperone / inclusion body / heat shock protein binding / ATP-dependent protein folding chaperone / ADP binding / unfolded protein binding / protein folding / protein-folding chaperone binding / response to heat / protein refolding / protein-containing complex assembly / DNA replication / protein domain specific binding / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex / zinc ion binding / ATP binding / membrane / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Harrison, C.J. / Kuriyan, J. | ||||||
![]() | ![]() Title: Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Authors: Harrison, C.J. / Hayer-Hartl, M. / Di Liberto, M. / Hartl, F. / Kuriyan, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 139.5 KB | Display | ![]() |
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PDB format | ![]() | 108.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.7 KB | Display | ![]() |
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Full document | ![]() | 500.3 KB | Display | |
Data in XML | ![]() | 31.7 KB | Display | |
Data in CIF | ![]() | 43 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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
#1: Protein | Mass: 21882.854 Da / Num. of mol.: 2 / Mutation: CHAIN A, B, G122D Source method: isolated from a genetically manipulated source Details: ELASTASE PROTEOLYSIS PRODUCT, RESIDUES 34 - 197 / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | | Mass: 41572.105 Da / Num. of mol.: 1 / Fragment: ATPASE DOMAIN RESIDUES 3 - 383 / Mutation: CHAIN D, P319L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.5 Å3/Da / Density % sol: 65 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.6 | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Oct 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 26024 / % possible obs: 95.7 % / Observed criterion σ(I): 0 / Redundancy: 29 % / Rsym value: 0.093 / Net I/σ(I): 18 |
Reflection shell | Resolution: 2.8→2.9 Å / Mean I/σ(I) obs: 7 / Rsym value: 0.179 / % possible all: 86.4 |
Reflection | *PLUS Num. measured all: 754420 / Rmerge(I) obs: 0.093 |
Reflection shell | *PLUS % possible obs: 86.4 % / Rmerge(I) obs: 0.179 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.8→30 Å
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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