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Open data
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Basic information
Entry | Database: PDB / ID: 1pv2 | ||||||
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Title | Native Form 2 E.coli Chaperone Hsp31 | ||||||
![]() | Chaperone protein hchA | ||||||
![]() | CHAPERONE / Heat Shock Protein / Putative Catalytic Triad / Flexibility / monoclinic | ||||||
Function / homology | ![]() D-lactate dehydratase / response to methylglyoxal / glyoxalase III activity / thiolester hydrolase activity / methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione / protein repair / guanine deglycation / protein deglycase / protein deglycase activity / RNA repair ...D-lactate dehydratase / response to methylglyoxal / glyoxalase III activity / thiolester hydrolase activity / methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione / protein repair / guanine deglycation / protein deglycase / protein deglycase activity / RNA repair / Hydrolases; Acting on ester bonds; Thioester hydrolases / response to acidic pH / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / DNA repair / protein homodimerization activity / zinc ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Quigley, P.M. / Korotkov, K. / Baneyx, F. / Hol, W.G.J. | ||||||
![]() | ![]() Title: A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Authors: Quigley, P.M. / Korotkov, K. / Baneyx, F. / Hol, W.G.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 | ![]() | 398.5 KB | Display | ![]() |
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PDB format | ![]() | 329.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 433.3 KB | Display | ![]() |
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Full document | ![]() | 485.4 KB | Display | |
Data in XML | ![]() | 43.2 KB | Display | |
Data in CIF | ![]() | 64.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1n57S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 31226.416 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.51 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 26% PEG 6000,50mM NaCl,100 mM Tris pH 7.5.5G, VAPOR DIFFUSION, SITTING DROP, temperature 22K, temperature 295K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 / 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: Jan 13, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.77 Å / Relative weight: 1 |
Reflection | Resolution: 2.71→48.8 Å / Num. all: 57067 / Num. obs: 57067 / % possible obs: 100 % / Observed criterion σ(I): 28 / Redundancy: 1.9 % / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 9.4 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.339 / Mean I/σ(I) obs: 2 / Num. unique all: 5883 / Rsym value: 0.339 / % possible all: 94.5 |
Reflection | *PLUS Highest resolution: 2.7 Å / Num. obs: 60105 / % possible obs: 96.1 % |
Reflection shell | *PLUS % possible obs: 94.1 % / Mean I/σ(I) obs: 2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1n57 Resolution: 2.71→48.8 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.863 / SU B: 16.066 / SU ML: 0.312 / Cross valid method: THROUGHOUT / ESU R Free: 0.421 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.455 Å2
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Refinement step | Cycle: LAST / Resolution: 2.71→48.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.707→2.777 Å / Total num. of bins used: 20 /
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 20 Å / Rfactor Rfree: 0.287 / Rfactor Rwork: 0.222 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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