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Yorodumi- PDB-1lqk: High Resolution Structure of Fosfomycin Resistance Protein A (FosA) -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lqk | ||||||
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Title | High Resolution Structure of Fosfomycin Resistance Protein A (FosA) | ||||||
Components | probable Fosfomycin Resistance Protein | ||||||
Keywords | TRANSFERASE / potassium binding loop / manganese binding | ||||||
Function / homology | Function and homology information glutathione transferase / glutathione transferase activity / response to antibiotic / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.35 Å | ||||||
Authors | Rife, C.L. / Pharris, R.E. / Newcomer, M.E. / Armstrong, R.N. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2002 Title: Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+) Authors: Rife, C.L. / Pharris, R.E. / Newcomer, M.E. / Armstrong, R.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lqk.cif.gz | 138.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lqk.ent.gz | 108.5 KB | Display | PDB format |
PDBx/mmJSON format | 1lqk.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lq/1lqk ftp://data.pdbj.org/pub/pdb/validation_reports/lq/1lqk | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The biological assembly is a dimer. |
-Components
#1: Protein | Mass: 15143.006 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Plasmid: pET-20 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21-DE3 / References: UniProt: Q9I4K6, glutathione transferase #2: Chemical | #3: Chemical | #4: Chemical | #5: 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: 2.01 Å3/Da / Density meas: 38.7 Mg/m3 / Density % sol: 47.24 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: WELL CONTAINED 40% PENTAERYTHRITOL PROPOXYLATE 629, 0.08M K2HPO4. DROP CONTAINED 0.002 M MNCL2, 0.002M FOSFOMYCIN, 10 MG/ML FOSA, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-D / Wavelength: 1.0062 / Wavelength: 1.0062 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 16, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0062 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→30 Å / Num. all: 55325 / Num. obs: 55325 / % possible obs: 92.6 % / Observed criterion σ(I): -3 / Redundancy: 6.1 % / Rmerge(I) obs: 0.03 / Net I/σ(I): 38.6 |
Reflection shell | Resolution: 1.35→1.4 Å / Rmerge(I) obs: 0.216 / Mean I/σ(I) obs: 5.3 / % possible all: 58.6 |
Reflection | *PLUS Lowest resolution: 30 Å / Rmerge(I) obs: 0.03 |
Reflection shell | *PLUS % possible obs: 58.6 % / Rmerge(I) obs: 0.22 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.35→30 Å / Num. parameters: 23217 / Num. restraintsaints: 28310 / Cross valid method: FREE R / σ(F): 4 / Stereochemistry target values: Engh & Huber / Details: Refmac was also used in refinement.
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 7 / Occupancy sum hydrogen: 1968 / Occupancy sum non hydrogen: 2526.55 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.35→30 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELX / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.138 / Rfactor Rwork: 0.1319 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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