+Open data
-Basic information
Entry | Database: PDB / ID: 3cs2 | ||||||
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Title | Crystal structure of PTE G60A mutant | ||||||
Components | Parathion hydrolase | ||||||
Keywords | HYDROLASE / Metal binding protein / METALLOENZYME / TIM BARREL / NERVE AGENTS / Membrane / Metal-binding | ||||||
Function / homology | Function and homology information aryldialkylphosphatase / aryldialkylphosphatase activity / catabolic process / zinc ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Brevundimonas diminuta (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Kim, J. / Almo, S.C. | ||||||
Citation | Journal: Biochemistry / Year: 2008 Title: Structure of diethyl phosphate bound to the binuclear metal center of phosphotriesterase. Authors: Kim, J. / Tsai, P.C. / Chen, S.L. / Himo, F. / Almo, S.C. / Raushel, F.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3cs2.cif.gz | 286.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3cs2.ent.gz | 228.8 KB | Display | PDB format |
PDBx/mmJSON format | 3cs2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3cs2_validation.pdf.gz | 468.1 KB | Display | wwPDB validaton report |
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Full document | 3cs2_full_validation.pdf.gz | 483.5 KB | Display | |
Data in XML | 3cs2_validation.xml.gz | 59.6 KB | Display | |
Data in CIF | 3cs2_validation.cif.gz | 88.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/3cs2 ftp://data.pdbj.org/pub/pdb/validation_reports/cs/3cs2 | HTTPS FTP |
-Related structure data
Related structure data | 2o4qC 3cakC 1p6bS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 35943.961 Da / Num. of mol.: 4 / Fragment: residues 34-364 / Mutation: G60A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Brevundimonas diminuta (bacteria) / Gene: opd / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: P0A434, aryldialkylphosphatase #2: Chemical | ChemComp-CAC / #3: Chemical | ChemComp-CO / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.14 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.2M Mg acetate, 0.1M Na-cacodylate, 20% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X3A / Wavelength: 0.97904 Å |
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Detector | Type: MAR CCD 165 mm / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97904 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→31.64 Å / Num. all: 91515 / Num. obs: 91515 / % possible obs: 96.3 % / Redundancy: 3 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 7.7 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.242 / Mean I/σ(I) obs: 3.39 / Num. unique all: 7663 / Rsym value: 0.286 / % possible all: 80.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1p6b Resolution: 1.95→31.64 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.925 / SU B: 3.634 / SU ML: 0.106 / Cross valid method: THROUGHOUT / ESU R: 0.175 / ESU R Free: 0.162 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.258 Å2
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Refinement step | Cycle: LAST / Resolution: 1.95→31.64 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.95→2.002 Å / Total num. of bins used: 20
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