+Open data
-Basic information
Entry | Database: PDB / ID: 1lqa | ||||||
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Title | TAS PROTEIN FROM ESCHERICHIA COLI IN COMPLEX WITH NADPH | ||||||
Components | Tas protein | ||||||
Keywords | OXIDOREDUCTASE / TIM barrel / Structure 2 Function Project / S2F / Structural Genomics | ||||||
Function / homology | Function and homology information aldo-keto reductase (NADPH) activity / cellular response to amino acid starvation / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.604 Å | ||||||
Authors | Obmolova, G. / Teplyakov, A. / Khil, P.P. / Howard, A.J. / Camerini-Otero, R.D. / Gilliland, G.L. / Structure 2 Function Project (S2F) | ||||||
Citation | Journal: PROTEINS: STRUCT.,FUNCT.,GENET. / Year: 2003 Title: Crystal structure of the Escherichia coli Tas protein, an NADP(H)-dependent aldo-keto reductase Authors: Obmolova, G. / Teplyakov, A. / Khil, P.P. / Howard, A.J. / Camerini-Otero, R.D. / Gilliland, G.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lqa.cif.gz | 167.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lqa.ent.gz | 131.3 KB | Display | PDB format |
PDBx/mmJSON format | 1lqa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lqa_validation.pdf.gz | 969.9 KB | Display | wwPDB validaton report |
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Full document | 1lqa_full_validation.pdf.gz | 976.5 KB | Display | |
Data in XML | 1lqa_validation.xml.gz | 35.5 KB | Display | |
Data in CIF | 1lqa_validation.cif.gz | 55.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lq/1lqa ftp://data.pdbj.org/pub/pdb/validation_reports/lq/1lqa | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 38544.434 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: Tas / Plasmid: pDEST14 / Cell line (production host): B834 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A9T4 #2: Chemical | #3: 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: 2.23 Å3/Da / Density % sol: 44.9 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.1M Tris, 15% PEG8000, 50mM Ammonium Sulfate, 0.2M Magnesium Chloride, 10mM NADPH, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1.0072 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 8, 2001 |
Radiation | Monochromator: Si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0072 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / Num. all: 84533 / Num. obs: 84533 / % possible obs: 92.6 % / Observed criterion σ(I): -3 / Redundancy: 6.3 % / Biso Wilson estimate: 14.5 Å2 / Rmerge(I) obs: 0.065 / Net I/σ(I): 23.8 |
Reflection shell | Resolution: 1.6→1.64 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.175 / Mean I/σ(I) obs: 4.1 / Num. unique all: 3455 / % possible all: 57.8 |
Reflection | *PLUS Num. obs: 160862 / % possible obs: 92 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.063 |
Reflection shell | *PLUS Mean I/σ(I) obs: 2.9 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.604→10 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.95 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Shrinkage radii: 0.8 Å / Solvent model: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.775 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.604→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.604→1.644 Å / Total num. of bins used: 20 /
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Refinement | *PLUS Highest resolution: 1.6 Å / % reflection Rfree: 3 % / Rfactor Rfree: 0.186 / Rfactor Rwork: 0.146 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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