+
Open data
-
Basic information
Entry | Database: PDB / ID: 1s3c | ||||||
---|---|---|---|---|---|---|---|
Title | ARSENATE REDUCTASE C12S 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 83.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 63 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 374.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 376.1 KB | Display | |
Data in XML | ![]() | 4.7 KB | Display | |
Data in CIF | ![]() | 8.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1s3dC ![]() 1sd8C ![]() 1sd9C ![]() 1sjzC ![]() 1sk0C ![]() 1sk1C ![]() 1sk2C C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||||||||
2 | ![]()
| |||||||||||||||
Unit cell |
| |||||||||||||||
Components on special symmetry positions |
|
-
Components
#1: Protein | Mass: 15833.175 Da / Num. of mol.: 1 / Mutation: C12S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli / Production host: ![]() ![]() References: UniProt: P08692, arsenate reductase (glutathione/glutaredoxin) | ||||
---|---|---|---|---|---|
#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.92 Å3/Da / Density % sol: 57.9 % |
---|---|
Crystal grow | Method: vapor diffusion, hanging drop / pH: 4.8 Details: CESIUM SULFATE, ACETATE, pH 4.8, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 93 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Monochromator: SI(111) DOUBLE-CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→20 Å / Num. obs: 71887 / % possible obs: 81.5 % / Observed criterion σ(I): -3 / Redundancy: 10.2 % / Rmerge(I) obs: 0.1172 / Rsym value: 0.1172 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 1.25→1.28 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.677 / Mean I/σ(I) obs: 0.62 / Rsym value: 0.677 / % possible all: 66 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: NATIVE STRUCTURE Resolution: 1.25→20 Å / Num. parameters: 12836 / Num. restraintsaints: 15250 / Cross valid method: THROUGHOUT / σ(F): 0 Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
| |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 10 / Occupancy sum hydrogen: 1112 / Occupancy sum non hydrogen: 1352.61 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.25→20 Å
| |||||||||||||||||||||||||||||||||
Refine LS restraints |
|