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- PDB-1lqp: CRYSTAL STRUCTURE OF THE FOSFOMYCIN RESISTANCE PROTEIN (FOSA) CON... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1lqp | ||||||
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Title | CRYSTAL STRUCTURE OF THE FOSFOMYCIN RESISTANCE PROTEIN (FOSA) CONTAINING BOUND SUBSTRATE | ||||||
![]() | PROBABLE FOSFOMYCIN RESISTANCE PROTEIN | ||||||
![]() | TRANSFERASE / potassium binding loop / manganese binding | ||||||
Function / homology | ![]() glutathione transferase / glutathione transferase activity / response to antibiotic / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rife, C.L. / Pharris, R.E. / Newcomer, M.E. / Armstrong, R.N. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 140.5 KB | Display | ![]() |
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PDB format | ![]() | 109.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 457.9 KB | Display | ![]() |
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Full document | ![]() | 465.2 KB | Display | |
Data in XML | ![]() | 17.9 KB | Display | |
Data in CIF | ![]() | 26.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1lqkSC ![]() 1lqoC S: Starting model for refinement 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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1 |
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Unit cell |
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Details | The biological assembly is a dimer of chains A and B |
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Components
#1: Protein | Mass: 15143.006 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-FCN / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.7 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: WELL CONTAINED 40% PENTAERYTHRITOL PROPOXYLATE 629, 0.10M KCL. 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: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 20, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.19→100 Å / Num. obs: 77910 / % possible obs: 86.3 % / Observed criterion σ(I): -3 / Redundancy: 8.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 15 |
Reflection shell | Resolution: 1.19→1.23 Å / Rmerge(I) obs: 0.31 / Mean I/σ(I) obs: 3.6 / % possible all: 57.8 |
Reflection | *PLUS Lowest resolution: 20 Å / % possible obs: 90.8 % / Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS % possible obs: 57.8 % / Rmerge(I) obs: 0.31 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1LQK Resolution: 1.19→20 Å / Num. parameters: 23565 / Num. restraintsaints: 28753 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 4%
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 6 / Occupancy sum hydrogen: 2007.4 / Occupancy sum non hydrogen: 2576 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.19→20 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.147 / Rfactor Rfree: 0.1893 / Rfactor Rwork: 0.1463 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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