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- PDB-1fpz: CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fpz | ||||||
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Title | CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE | ||||||
![]() | CYCLIN-DEPENDENT KINASE INHIBITOR 3 | ||||||
![]() | HYDROLASE / alpha-beta sandwich | ||||||
Function / homology | ![]() protein tyrosine/serine/threonine phosphatase activity / myosin phosphatase activity / regulation of cyclin-dependent protein serine/threonine kinase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / G1/S transition of mitotic cell cycle / regulation of cell cycle ...protein tyrosine/serine/threonine phosphatase activity / myosin phosphatase activity / regulation of cyclin-dependent protein serine/threonine kinase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity / G1/S transition of mitotic cell cycle / regulation of cell cycle / negative regulation of cell population proliferation / perinuclear region of cytoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Song, H. / Hanlon, N. / Brown, N.R. / Noble, M.E.M. / Johnson, L.N. / Barford, D. | ||||||
![]() | ![]() Title: Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Authors: Song, H. / Hanlon, N. / Brown, N.R. / Noble, M.E. / Johnson, L.N. / Barford, D. #1: ![]() Title: Cdi1, a human G1 and S phase protein phosphatase that associates with Cdk2 Authors: Gyruris, J. / Golemis, E. / Chertkov, H. / Brent, R. #2: ![]() Title: The p21Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases Authors: Harper, J.W. / Adami, G.R. / Wei, N. / Keyomarsi, K. / Elledge, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 230.6 KB | Display | ![]() |
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PDB format | ![]() | 186.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480 KB | Display | ![]() |
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Full document | ![]() | 536.8 KB | Display | |
Data in XML | ![]() | 54 KB | Display | |
Data in CIF | ![]() | 76.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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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3 | ![]()
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4 | ![]()
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5 | ![]()
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6 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 23819.057 Da / Num. of mol.: 6 / Mutation: C140S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50.09 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5 Details: PEG 8000, ammonium sulphate, sodium acetate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Details: Hanlon, N., (1998) Protein Sci., 7, 508. | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC / Detector: CCD / Date: Jan 1, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 90055 / % possible obs: 96.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Biso Wilson estimate: 23.6 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 2→2.12 Å / Rmerge(I) obs: 0.38 / % possible all: 91.6 |
Reflection | *PLUS Num. measured all: 319770 |
Reflection shell | *PLUS % possible obs: 91.6 % / Mean I/σ(I) obs: 1.9 |
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Processing
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Refinement | Resolution: 2→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.202 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |