+Open data
-Basic information
Entry | Database: PDB / ID: 2o8g | ||||||
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Title | Rat pp1c gamma complexed with mouse inhibitor-2 | ||||||
Components |
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Keywords | HYDROLASE/INHIBITOR / protein phosphatase / inhibitor-2 / HYDROLASE-INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / RHO GTPases Activate Formins / RAF activation / Separation of Sister Chromatids / PTW/PP1 phosphatase complex / regulation of nucleocytoplasmic transport / protein phosphatase 1 binding ...Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / RHO GTPases Activate Formins / RAF activation / Separation of Sister Chromatids / PTW/PP1 phosphatase complex / regulation of nucleocytoplasmic transport / protein phosphatase 1 binding / lamin binding / microtubule organizing center / protein phosphatase inhibitor activity / myosin phosphatase activity / molecular function inhibitor activity / glycogen metabolic process / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / entrainment of circadian clock by photoperiod / phosphatase activity / cleavage furrow / blastocyst development / regulation of signal transduction / positive regulation of glial cell proliferation / protein dephosphorylation / circadian regulation of gene expression / regulation of circadian rhythm / neuron differentiation / kinetochore / presynapse / midbody / growth cone / spermatogenesis / protein phosphatase binding / mitochondrial outer membrane / postsynapse / dendritic spine / chromosome, telomeric region / nuclear speck / protein domain specific binding / cell division / glutamatergic synapse / protein-containing complex binding / nucleolus / protein kinase binding / protein-containing complex / mitochondrion / nucleus / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Hurley, T.D. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: Structural basis for regulation of protein phosphatase 1 by inhibitor-2. Authors: Hurley, T.D. / Yang, J. / Zhang, L. / Goodwin, K.D. / Zou, Q. / Cortese, M. / Dunker, A.K. / Depaoli-Roach, A.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2o8g.cif.gz | 164.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2o8g.ent.gz | 126 KB | Display | PDB format |
PDBx/mmJSON format | 2o8g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2o8g_validation.pdf.gz | 461.4 KB | Display | wwPDB validaton report |
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Full document | 2o8g_full_validation.pdf.gz | 473.3 KB | Display | |
Data in XML | 2o8g_validation.xml.gz | 28.4 KB | Display | |
Data in CIF | 2o8g_validation.cif.gz | 40.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o8/2o8g ftp://data.pdbj.org/pub/pdb/validation_reports/o8/2o8g | HTTPS FTP |
-Related structure data
Related structure data | 2o8aSC S: Starting model for refinement C: citing same article (ref.) |
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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: 37859.648 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Ppp1cc / Plasmid: pTACTAC / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 References: UniProt: P63088, protein-serine/threonine phosphatase #2: Protein | Mass: 23152.285 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ppp1r2 / Plasmid: pACYC / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9DCL8 #3: Chemical | #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: 3.05 Å3/Da / Density % sol: 59.7 % |
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, sitting drop / pH: 8.6 Details: 100 mM Tris-HCL, 150 mM Sodium Citrate, 20% (w/v) PEG 3350, pH 8.6, VAPOR DIFFUSION, SITTING DROP, temperature 288K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.98 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 10, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. all: 52428 / Num. obs: 52166 / % possible obs: 99.5 % / Observed criterion σ(I): 0.2 / Redundancy: 5.4 % / Biso Wilson estimate: 56 Å2 / Rmerge(I) obs: 0.09 / Χ2: 1.053 / Net I/σ(I): 8.7 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.61 / Mean I/σ(I) obs: 1.9 / Num. unique all: 4949 / Χ2: 1.014 / % possible all: 95.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 2O8A Resolution: 2.5→48.8 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.92 / SU B: 6.347 / SU ML: 0.142 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.24 / ESU R Free: 0.208 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.687 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→48.8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.565 Å / Total num. of bins used: 20
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