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Yorodumi- PDB-5jnr: Crystal structure of human low molecular weight protein tyrosine ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5jnr | ||||||
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Title | Crystal structure of human low molecular weight protein tyrosine phosphatase (LMPTP) type A | ||||||
Components | Low molecular weight phosphotyrosine protein phosphatase | ||||||
Keywords | HYDROLASE / protein tyrosine phosphatase / LMW-PTP / LMPTP | ||||||
Function / homology | Function and homology information acid phosphatase / acid phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / sarcolemma / cytoplasmic side of plasma membrane / extracellular exosome / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Stanford, S.M. / Aleshin, A.E. / Liddington, R.C. / Bankston, L. / Cadwell, G. / Bottini, N. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nat. Chem. Biol. / Year: 2017 Title: Diabetes reversal by inhibition of the low-molecular-weight tyrosine phosphatase. Authors: Stanford, S.M. / Aleshin, A.E. / Zhang, V. / Ardecky, R.J. / Hedrick, M.P. / Zou, J. / Ganji, S.R. / Bliss, M.R. / Yamamoto, F. / Bobkov, A.A. / Kiselar, J. / Liu, Y. / Cadwell, G.W. / ...Authors: Stanford, S.M. / Aleshin, A.E. / Zhang, V. / Ardecky, R.J. / Hedrick, M.P. / Zou, J. / Ganji, S.R. / Bliss, M.R. / Yamamoto, F. / Bobkov, A.A. / Kiselar, J. / Liu, Y. / Cadwell, G.W. / Khare, S. / Yu, J. / Barquilla, A. / Chung, T.D.Y. / Mustelin, T. / Schenk, S. / Bankston, L.A. / Liddington, R.C. / Pinkerton, A.B. / Bottini, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5jnr.cif.gz | 51.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5jnr.ent.gz | 35.2 KB | Display | PDB format |
PDBx/mmJSON format | 5jnr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jn/5jnr ftp://data.pdbj.org/pub/pdb/validation_reports/jn/5jnr | HTTPS FTP |
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-Related structure data
Related structure data | 5jnsC 5jntC 5jnuC 5jnvC 5jnwC 3n8iS C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 18209.635 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACP1 / Plasmid: pGEX-4T / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P24666, protein-tyrosine-phosphatase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.69 % / Mosaicity: 0.48 ° |
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Crystal grow | Temperature: 293 K / Method: evaporation / pH: 5.5 / Details: 7% PEG 10K, Bis Tris, Ammonium Acetate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1.5418 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 14, 2014 |
Radiation | Monochromator: mirrows / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→36.51 Å / Num. obs: 12105 / % possible obs: 96.9 % / Redundancy: 3.8 % / CC1/2: 0.997 / Rmerge(I) obs: 0.064 / Net I/σ(I): 34 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.238 / % possible all: 91.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3N8I Resolution: 2→36.51 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.927 / SU B: 3.807 / SU ML: 0.105 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.176 / ESU R Free: 0.159 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 74.95 Å2 / Biso mean: 25.942 Å2 / Biso min: 7.94 Å2
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Refinement step | Cycle: final / Resolution: 2→36.51 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.995→2.047 Å / Total num. of bins used: 20
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