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Open data
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Basic information
Entry | Database: PDB / ID: 1nbw | ||||||
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Title | Glycerol dehydratase reactivase | ||||||
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![]() | HYDROLASE / Glycerol dehydratase / Reactivase / Molecular chaperone / Actin-like ATPase domain / beta/beta/alpha swiveling domain | ||||||
Function / homology | ![]() glycerol dehydratase / glycerol dehydratase activity / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liao, D.-I. / Reiss, L. / Turner Jr., I. / Dotson, G. | ||||||
![]() | ![]() Title: Structure of glycerol dehydratase reactivase: A new type of molecular chaperone Authors: Liao, D.-I. / Reiss, L. / Turner Jr., I. / Dotson, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 275.1 KB | Display | ![]() |
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PDB format | ![]() | 229.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 389.5 KB | Display | ![]() |
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Full document | ![]() | 423.6 KB | Display | |
Data in XML | ![]() | 30.9 KB | Display | |
Data in CIF | ![]() | 49.8 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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Details | The biological assembly of glycerol dehydratase reactivase is a heterotetramer. The asymmetric unit of the crystal contains an entire heterotetramer. It consists of two copies of alpha-beta heterodimers related by a non-crystallographic two fold symmetry. Chain names for the two alpha subunits are A and C, those for the beta subunits are B and D. |
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Components
#1: Protein | Mass: 63650.156 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 12005.414 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.32 Å3/Da / Density % sol: 62.94 % | ||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: Na Acetate, Imidazole, CaCl2, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||
Crystal grow | *PLUS PH range low: 6.6 / PH range high: 6.5 | ||||||||||||||||||||||||||||
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: MARRESEARCH / Detector: CCD / Date: Sep 15, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→30 Å / Num. all: 79404 / Num. obs: 79404 / % possible obs: 98.2 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 29.3 |
Reflection shell | Resolution: 2.4→2.44 Å / Rmerge(I) obs: 0.206 / Mean I/σ(I) obs: 4.4 / % possible all: 82.4 |
Reflection | *PLUS Num. measured all: 534068 |
Reflection shell | *PLUS % possible obs: 82.4 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 39.4 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→30 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 30 Å / % reflection Rfree: 5 % | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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