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Open data
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Basic information
Entry | Database: PDB / ID: 1sjz | ||||||
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Title | ARSENATE REDUCTASE R60K MUTANT +0.4M ARSENITE FROM E. COLI | ||||||
![]() | Arsenate reductase | ||||||
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Function / homology | ![]() arsenate reductase (glutathione/glutaredoxin) / ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Demel, S. / Edwards, B.F. | ||||||
![]() | ![]() Title: Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product. Authors: DeMel, S. / Shi, J. / Martin, P. / Rosen, B.P. / Edwards, B.F. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.2 KB | Display | ![]() |
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PDB format | ![]() | 35 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1s3cC ![]() 1s3dC ![]() 1sd8C ![]() 1sd9C ![]() 1sk0C ![]() 1sk1C ![]() 1sk2C C: citing same article ( |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 15799.976 Da / Num. of mol.: 1 / Mutation: R60K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P08692, arsenate reductase (glutathione/glutaredoxin) | ||||||
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#2: Chemical | ![]() #3: Chemical | #4: Chemical | ChemComp-TAS / | ![]() #5: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 58 % |
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Crystal grow![]() | Temperature: 278 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: 50% saturated Cesium Sulfate, 100mM sodium acetate,5mM DTT, pH 4.80, VAPOR DIFFUSION, HANGING DROP, temperature 278K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 9, 2001 / Details: OSMIC MIRRORS |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.55→20 Å / Num. obs: 35645 / % possible obs: 93.5 % / Observed criterion σ(I): -3 / Redundancy: 16.3 % / Rmerge(I) obs: 0.1471 / Rsym value: 0.1471 / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 1.55→1.61 Å / Redundancy: 3.71 % / Rmerge(I) obs: 0.5123 / Mean I/σ(I) obs: 1.561 / Rsym value: 0.5123 / % possible all: 60.45 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: NATIVE STRUCTURE Resolution: 1.8→20 Å / Num. parameters: 5998 / Num. restraintsaints: 4594 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 4 / Occupancy sum hydrogen: 0 / Occupancy sum non hydrogen: 1456.91 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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