+Open data
-Basic information
Entry | Database: PDB / ID: 1zck | ||||||
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Title | native structure prl-1 (ptp4a1) | ||||||
Components | protein tyrosine phosphatase 4a1 | ||||||
Keywords | HYDROLASE / prl-1 ptp4a1 | ||||||
Function / homology | Function and homology information protein tyrosine/serine/threonine phosphatase activity / dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / cytoplasmic side of plasma membrane / spindle / early endosome / positive regulation of cell migration / cell cycle / endoplasmic reticulum ...protein tyrosine/serine/threonine phosphatase activity / dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / cytoplasmic side of plasma membrane / spindle / early endosome / positive regulation of cell migration / cell cycle / endoplasmic reticulum / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.9 Å | ||||||
Authors | Sun, J.P. / Wang, W.Q. / Yang, H. / Liu, S. / Liang, F. / Fedorov, A.A. / Almo, S.C. / Zhang, Z.Y. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Structure and Biochemical Properties of PRL-1, a Phosphatase Implicated in Cell Growth, Differentiation, and Tumor Invasion. Authors: Sun, J.P. / Wang, W.Q. / Yang, H. / Liu, S. / Liang, F. / Fedorov, A.A. / Almo, S.C. / Zhang, Z.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zck.cif.gz | 103.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zck.ent.gz | 85.4 KB | Display | PDB format |
PDBx/mmJSON format | 1zck.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zc/1zck ftp://data.pdbj.org/pub/pdb/validation_reports/zc/1zck | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 17750.221 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pGEX / Production host: Escherichia coli (E. coli) / Strain (production host): BL843 / References: UniProt: Q78EG7 #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: 3.2 Å3/Da / Density % sol: 61.61 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.8 Details: Ammonium Sulfate, Sodium Acetate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 200 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.9800, 0.97849, 0.96261 | ||||||||||||
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 30, 2003 | ||||||||||||
Radiation | Monochromator: Si 111 CHANNEL / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.9→30 Å / Num. obs: 48966 / % possible obs: 96.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 | ||||||||||||
Reflection shell | Resolution: 1.9→1.97 Å / % possible all: 88.6 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.9→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
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