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- PDB-1c0e: Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase -
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Open data
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Basic information
Entry | Database: PDB / ID: 1c0e | ||||||
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Title | Active Site S19A Mutant of Bovine Heart Phosphotyrosyl Phosphatase | ||||||
![]() | PROTEIN (TYROSINE PHOSPHATASE (ORTHOPHOSPHORIC MONOESTER PHOSPHOHYDROLASE)) | ||||||
![]() | HYDROLASE / TYROSINE PHOSPHATASE / PHOSPHATASE DIMER | ||||||
Function / homology | ![]() acid phosphatase / acid phosphatase activity / non-membrane spanning protein tyrosine phosphatase activity / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Tabernero, L. / Evans, B.N. / Tishmack, P.A. / Van Etten, R.L. / Stauffacher, C.V. | ||||||
![]() | ![]() Title: The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. Authors: Tabernero, L. / Evans, B.N. / Tishmack, P.A. / Van Etten, R.L. / Stauffacher, C.V. #1: ![]() Title: Structure of Bovine Heart Phosphotyrosyl Phosphatase at 2.2 Angstroms Resolution Authors: Zhang, M. / Van Etten, R.L. / Stauffacher, C.V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 73.1 KB | Display | ![]() |
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PDB format | ![]() | 56.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 389.6 KB | Display | ![]() |
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Full document | ![]() | 398 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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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: 17930.326 Da / Num. of mol.: 2 / Mutation: S19A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.13 % | ||||||||||||||||||||
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Crystal grow | pH: 7 / Details: PEG 4000, TRIS BUFFER, pH 7.00 | ||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: unknown / Details: used to seeding | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jan 15, 1995 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→30 Å / Num. obs: 15625 / % possible obs: 93.4 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 15 |
Reflection shell | Resolution: 2.2→2.3 Å / Redundancy: 1 % / Rmerge(I) obs: 0.306 / % possible all: 67.7 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 30 Å / Observed criterion σ(I): 0 / Redundancy: 3 % |
Reflection shell | *PLUS Redundancy: 1 % |
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Processing
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Refinement | Resolution: 2.2→20 Å / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2.2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |