+Open data
-Basic information
Entry | Database: PDB / ID: 1g5b | ||||||
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Title | BACTERIOPHAGE LAMBDA SER/THR PROTEIN PHOSPHATASE | ||||||
Components | SERINE/THREONINE PROTEIN PHOSPHATASESerine/threonine-specific protein kinase | ||||||
Keywords | Viral protein / hydrolase / Bacteriophage Lambda / Ser/Thr Protein Phosphatase / PPase / Protein Phosphatase / Manganese / Sulfate | ||||||
Function / homology | Function and homology information protein-serine/threonine phosphatase / phosphoprotein phosphatase activity / metal ion binding Similarity search - Function | ||||||
Biological species | Enterobacteria phage lambda (virus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.15 Å | ||||||
Authors | Voegtli, W.C. / White, D.J. / Reiter, N.J. / Rusnak, F. / Rosenzweig, A.C. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Authors: Voegtli, W.C. / White, D.J. / Reiter, N.J. / Rusnak, F. / Rosenzweig, A.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g5b.cif.gz | 150.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g5b.ent.gz | 119.2 KB | Display | PDB format |
PDBx/mmJSON format | 1g5b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g5/1g5b ftp://data.pdbj.org/pub/pdb/validation_reports/g5/1g5b | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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Details | Biological assembly is a monomer |
-Components
#1: Protein | Mass: 25191.723 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage lambda (virus) / Genus: Lambda-like viruses / Plasmid: PT7-7 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P03772, Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases #2: Chemical | ChemComp-MN / #3: Chemical | #4: Chemical | ChemComp-SO4 / #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: 3.72 Å3/Da / Density % sol: 66.93 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 100 mM MES, 20% PEG 4000, 350 mM Ammonium Sulfate, 10 mM Manganese(II) Chloride, 50 mM Ammonium Acetate, 20 mM Dithiothreitol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 23K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 5ID-B / Wavelength: 0.99188, 1.0098, 1.0247 | ||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 4, 1999 | ||||||||||||
Radiation | Monochromator: Double Crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.15→30 Å / Num. all: 61694 / Num. obs: 61405 / % possible obs: 99.5 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4 % / Biso Wilson estimate: 27.4 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 10.6 | ||||||||||||
Reflection shell | Resolution: 2.15→2.19 Å / Redundancy: 4 % / Rmerge(I) obs: 0.316 / Mean I/σ(I) obs: 2.4 / % possible all: 99.5 | ||||||||||||
Reflection | *PLUS Num. measured all: 435477 | ||||||||||||
Reflection shell | *PLUS % possible obs: 99.6 % |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.15→35 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 250651.17 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh and Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 61.65 Å2 / ksol: 0.391 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.15→35 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.28 Å / Rfactor Rfree error: 0.013 / Total num. of bins used: 6
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 35 Å / σ(F): 0 / % reflection Rfree: 4.9 % / Rfactor Rwork: 0.2 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 42.7 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.268 / % reflection Rfree: 5 % / Rfactor Rwork: 0.249 |