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Yorodumi- PDB-1a6q: CRYSTAL STRUCTURE OF THE PROTEIN SERINE/THREONINE PHOSPHATASE 2C ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1a6q | |||||||||
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Title | CRYSTAL STRUCTURE OF THE PROTEIN SERINE/THREONINE PHOSPHATASE 2C AT 2 A RESOLUTION | |||||||||
Components | PHOSPHATASE 2C | |||||||||
Keywords | HYDROLASE / CATALYTIC MECHANISM / METALLOENZYME / PROTEIN PHOSPHATASE 2C / SIGNAL TRANSDUCTUIN | |||||||||
Function / homology | Function and homology information N-terminal protein myristoylation / calmodulin-dependent protein phosphatase activity / peptidyl-threonine dephosphorylation / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of non-canonical NF-kappaB signal transduction / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / R-SMAD binding / negative regulation of BMP signaling pathway ...N-terminal protein myristoylation / calmodulin-dependent protein phosphatase activity / peptidyl-threonine dephosphorylation / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of non-canonical NF-kappaB signal transduction / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / R-SMAD binding / negative regulation of BMP signaling pathway / dephosphorylation / negative regulation of canonical NF-kappaB signal transduction / cellular response to transforming growth factor beta stimulus / protein export from nucleus / protein dephosphorylation / positive regulation of protein export from nucleus / Downregulation of SMAD2/3:SMAD4 transcriptional activity / negative regulation of transforming growth factor beta receptor signaling pathway / positive regulation of canonical Wnt signaling pathway / manganese ion binding / positive regulation of canonical NF-kappaB signal transduction / regulation of cell cycle / positive regulation of DNA-templated transcription / magnesium ion binding / negative regulation of transcription by RNA polymerase II / nucleoplasm / membrane / nucleus / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2 Å | |||||||||
Authors | Das, A.K. / Helps, N.R. / Cohen, P.T.W. / Barford, D. | |||||||||
Citation | Journal: EMBO J. / Year: 1996 Title: Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. Authors: Das, A.K. / Helps, N.R. / Cohen, P.T. / Barford, D. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a6q.cif.gz | 83.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a6q.ent.gz | 65.4 KB | Display | PDB format |
PDBx/mmJSON format | 1a6q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a6/1a6q ftp://data.pdbj.org/pub/pdb/validation_reports/a6/1a6q | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 42502.703 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) References: UniProt: P35813, protein-serine/threonine phosphatase | ||||
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#2: Chemical | #3: Chemical | ChemComp-PO4 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 5 |
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-Sample preparation
Crystal | Density Matthews: 2.97 Å3/Da / Density % sol: 59 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / pH: 5 Details: 8-12% PEG8K,15% GLYCEROL, 50MM K-PO4, PH=5.0, 2 MM DTT AT 4 DEGREES C, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / Method: vapor diffusionDetails: drop solution was mixed with an equal volume of reservoir solution | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: ESRF / Beamline: BL19 / Wavelength: 0.87 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 9, 1996 / Details: MIRRORS |
Radiation | Monochromator: DARESBURY / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. obs: 33176 / % possible obs: 95.5 % / Observed criterion σ(I): 2 / Redundancy: 6.5 % / Rmerge(I) obs: 0.089 / Rsym value: 0.089 / Net I/σ(I): 12.6 |
Reflection | *PLUS Num. measured all: 215022 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2→6 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.82 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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