+Open data
-Basic information
Entry | Database: PDB / ID: 2v0p | ||||||
---|---|---|---|---|---|---|---|
Title | The Structure of Tap42 Alpha4 Subunit | ||||||
Components | TYPE 2A PHOSPHATASE-ASSOCIATED PROTEIN 42 | ||||||
Keywords | HYDROLASE INHIBITOR / PHOSPHORYLATION / SIGNAL TRANSDUCTION INHIBITOR | ||||||
Function / homology | Function and homology information regulation of dephosphorylation / extrinsic component of membrane / positive regulation of transcription by RNA polymerase I / TOR signaling / negative regulation of signal transduction / protein phosphatase 2A binding / cytosol Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.8 Å | ||||||
Authors | Roe, S.M. / Yang, J. / Barford, D. | ||||||
Citation | Journal: Biochemistry / Year: 2007 Title: The Structure of Tap42/Alpha4 Reveals a Tetratricopeptide Repeat-Like Fold and Provides Insights Into Pp2A Regulation. Authors: Yang, J. / Roe, S.M. / Prickett, T.D. / Brautigan, D.L. / Barford, D. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2v0p.cif.gz | 101 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2v0p.ent.gz | 83.5 KB | Display | PDB format |
PDBx/mmJSON format | 2v0p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2v0p_validation.pdf.gz | 433.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2v0p_full_validation.pdf.gz | 439.3 KB | Display | |
Data in XML | 2v0p_validation.xml.gz | 20.1 KB | Display | |
Data in CIF | 2v0p_validation.cif.gz | 29.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v0/2v0p ftp://data.pdbj.org/pub/pdb/validation_reports/v0/2v0p | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 27566.816 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-234 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): B834 / References: UniProt: Q04372 #2: Chemical | ChemComp-ZN / #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: THE PROTEIN WAS CONCENTRATED TO 10 MG/ML BEFORE CRYSTALLIZATION. CRYSTALS WERE GROWN AT 20C USING THE HANGING DROP METHOD. ONE MICROLITRE OF PROTEIN WAS MIXED WITH AN EQUAL VOLUME OF ...Details: THE PROTEIN WAS CONCENTRATED TO 10 MG/ML BEFORE CRYSTALLIZATION. CRYSTALS WERE GROWN AT 20C USING THE HANGING DROP METHOD. ONE MICROLITRE OF PROTEIN WAS MIXED WITH AN EQUAL VOLUME OF CRYSTALLIZATION BUFFER: 20% (W/V) PEG 8000, 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M MAGNESIUM ACETATE AND 2MM DTT. CRYSTALS WERE OPTIMISED BY SEEDING. |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9775 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 1, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9775 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 49867 / % possible obs: 96.4 % / Redundancy: 4.4 % / Biso Wilson estimate: 26.4 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 15.6 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.6 / % possible all: 96.4 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: SAD / Resolution: 1.8→71.07 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.936 / SU B: 7.611 / SU ML: 0.115 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.158 / ESU R Free: 0.138 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39.1 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→71.07 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|