+Open data
-Basic information
Entry | Database: PDB / ID: 1ljl | ||||||
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Title | Wild Type pI258 S. aureus arsenate reductase | ||||||
Components | arsenate reductase | ||||||
Keywords | OXIDOREDUCTASE / P-loop | ||||||
Function / homology | Function and homology information 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 | Staphylococcus aureus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.01 Å | ||||||
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. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2002 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ljl.cif.gz | 41.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ljl.ent.gz | 28 KB | Display | PDB format |
PDBx/mmJSON format | 1ljl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ljl_validation.pdf.gz | 421.3 KB | Display | wwPDB validaton report |
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Full document | 1ljl_full_validation.pdf.gz | 421.4 KB | Display | |
Data in XML | 1ljl_validation.xml.gz | 8.1 KB | Display | |
Data in CIF | 1ljl_validation.cif.gz | 10.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lj/1ljl ftp://data.pdbj.org/pub/pdb/validation_reports/lj/1ljl | HTTPS FTP |
-Related structure data
Related structure data | 1ljuC 1lk0C 1jf8S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14831.739 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: reduced / Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: arsc / Plasmid: pTrc99 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P0A006, EC: 1.97.1.5 |
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#2: Chemical | ChemComp-K / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.81 Å3/Da / Density % sol: 31.98 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: PEG4000, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 393K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Jan 15, 2002 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. all: 7503 / Num. obs: 7503 / % possible obs: 96 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Biso Wilson estimate: 25.9 Å2 / Rsym value: 0.07 / Net I/σ(I): 22.6 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 5 % / Mean I/σ(I) obs: 3.05 / Num. unique all: 751 / Rsym value: 0.43 / % possible all: 74.8 |
Reflection | *PLUS Lowest resolution: 15 Å / % possible obs: 96.5 % / Num. measured all: 203478 / Rmerge(I) obs: 0.07 |
Reflection shell | *PLUS % possible obs: 74.8 % / Rmerge(I) obs: 0.451 / Mean I/σ(I) obs: 3.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1JF8 Resolution: 2.01→14.96 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.01→14.96 Å
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 15 Å / Rfactor all: 0.23 / Rfactor Rfree: 0.254 / Rfactor Rwork: 0.214 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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