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- PDB-3r07: Structural analysis of an archaeal lipoylation system. A bi-parti... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3r07 | ||||||
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Title | Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum | ||||||
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![]() | TRANSFERASE / Adenylate-forming enzyme / Ligase / bi-partite / ATP-binding | ||||||
Function / homology | ![]() lipoate-protein ligase / lipoate-protein ligase activity / lipoic acid binding / protein lipoylation / ligase activity / protein-containing complex / ATP binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Posner, M.G. / Upadhyay, U. / Crennell, S. | ||||||
![]() | ![]() Title: Structural analysis of an archaeal lipoylation system. A bi-partite lipoate protein ligase and its E2 lipoyl domain from Thermoplasma acidophilum Authors: Posner, M.G. / Upadhyay, A. / Crennell, S. / Danson, M.J. / Bagby, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.3 KB | Display | ![]() |
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PDB format | ![]() | 64.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 460.2 KB | Display | ![]() |
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Full document | ![]() | 467.1 KB | Display | |
Data in XML | ![]() | 15.6 KB | Display | |
Data in CIF | ![]() | 21 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2arsS 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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Unit cell |
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Components
#1: Protein | Mass: 32695.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Co-expression Source: (gene. exp.) ![]() ![]() Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165 Gene: lplA, Ta0514 / Plasmid: pET19b / Production host: ![]() ![]() | ||||
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#2: Protein | Mass: 10561.207 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Co-expression Source: (gene. exp.) ![]() ![]() Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165 Gene: Ta0513, Ta0513m / Plasmid: pET28a / Production host: ![]() ![]() | ||||
#3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.42 Å3/Da / Density % sol: 64.04 % |
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Crystal grow | Temperature: 291 K / pH: 4.6 Details: 40% v/v MPD, 0.1M sodium acetate, 0.02M calcium chloride, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Oct 26, 2009 / Details: VORTEX FLUORESCENCE DETECTOR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→38.81 Å |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2ARS Resolution: 2.7→38.81 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.892 / SU B: 9.005 / SU ML: 0.192 / Cross valid method: THROUGHOUT / ESU R Free: 0.305 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 51.56 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→38.81 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.77 Å / Total num. of bins used: 20
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