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Open data
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Basic information
Entry | Database: PDB / ID: 1lk0 | ||||||
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Title | Disulfide intermediate of C89L Arsenate reductase from pI258 | ||||||
![]() | arsenate reductase | ||||||
![]() | OXIDOREDUCTASE / PTPase I fold / P-loop / disulfide cascade | ||||||
Function / homology | ![]() arsenate reductase (thioredoxin) / arsenate reductase (thioredoxin) activity / response to arsenic-containing substance / protein tyrosine phosphatase activity / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Messens, J. / Martins, J.C. / Van Belle, K. / Brosens, E. / Desmyter, A. / De Gieter, M. / Wieruszeski, J.M. / Willem, R. / Wyns, L. / Zegers, I. | ||||||
![]() | ![]() Title: All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade. Authors: Messens, J. / Martins, J.C. / Van Belle, K. / Brosens, E. / Desmyter, A. / De Gieter, M. / Wieruszeski, J.M. / Willem, R. / Wyns, L. / Zegers, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.2 KB | Display | ![]() |
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PDB format | ![]() | 54.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.7 KB | Display | ![]() |
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Full document | ![]() | 436.8 KB | Display | |
Data in XML | ![]() | 16.9 KB | Display | |
Data in CIF | ![]() | 25.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ljlC ![]() 1ljuC ![]() 1jf8S C: citing same article ( 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 14841.753 Da / Num. of mol.: 2 / Mutation: C89L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG4000, Tris, KCl, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8 | ||||||||||||||||||||||||||||||||||||||||||
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: Oct 26, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.6→25 Å / Num. obs: 31235 / % possible obs: 97.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rsym value: 0.033 |
Reflection shell | Resolution: 1.6→1.66 Å / Rmerge(I) obs: 0.065 / % possible all: 97.6 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. obs: 32094 / Num. measured all: 214661 / Rmerge(I) obs: 0.033 |
Reflection shell | *PLUS % possible obs: 97.6 % / Mean I/σ(I) obs: 14.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: C10SC15A ArsC (PDB ENTRY 1JF8) Resolution: 1.6→27.8 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.6→27.8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.6 Å / Lowest resolution: 30 Å / Rfactor Rfree: 0.234 / Rfactor Rwork: 0.22 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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