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Open data
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Basic information
Entry | Database: PDB / ID: 1s3d | |||||||||
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Title | ARSENATE REDUCTASE R60A MUTANT FROM E. COLI | |||||||||
![]() | Arsenate reductase | |||||||||
![]() | OXIDOREDUCTASE / ARSC / REDUCTASE / ARSENITE / ARSENATE | |||||||||
Function / homology | ![]() arsenate reductase (glutathione/glutaredoxin) / arsenate reductase (glutaredoxin) activity / response to arsenic-containing substance 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. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 87.4 KB | Display | ![]() |
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PDB format | ![]() | 65.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 378.7 KB | Display | ![]() |
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Full document | ![]() | 379.7 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 8.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1s3cC ![]() 1sd8C ![]() 1sd9C ![]() 1sjzC ![]() 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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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 15415.670 Da / Num. of mol.: 1 / Mutation: R60A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P08692, arsenate reductase (glutathione/glutaredoxin) | ||||
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#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-CS / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 57.1 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 4.8 Details: 50% Saturated Cesium sulfate, 100 mM sodium acetate, 5 mM DTT, pH 4.80, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 24, 2001 / Details: OSMIC MIRRORS |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.5287→20 Å / Num. obs: 34567 / % possible obs: 92.6 % / Observed criterion σ(I): -3 / Redundancy: 16.38 % / Rmerge(I) obs: 0.093 / Rsym value: 0.093 / Net I/σ(I): 25.1 |
Reflection shell | Resolution: 1.5287→1.588 Å / Redundancy: 3.92 % / Rmerge(I) obs: 0.2972 / Mean I/σ(I) obs: 3.13 / Rsym value: 0.2972 / % possible all: 56.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NATIVE STRUCTURE Resolution: 1.54→20 Å / Num. parameters: 13495 / Num. restraintsaints: 15505 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 9 / Occupancy sum hydrogen: 1103 / Occupancy sum non hydrogen: 1448.74 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.54→20 Å
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Refine LS restraints |
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