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- PDB-2w7r: Structure of the PDZ domain of Human Microtubule associated serin... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2w7r | ||||||
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Title | Structure of the PDZ domain of Human Microtubule associated serine- threonine kinase 4 | ||||||
![]() | MICROTUBULE-ASSOCIATED SERINE/THREONINE-PROTEIN KINASE 4 | ||||||
![]() | TRANSFERASE | ||||||
Function / homology | ![]() cytoskeleton organization / non-specific serine/threonine protein kinase / intracellular signal transduction / protein serine kinase activity / protein serine/threonine kinase activity / magnesium ion binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Muniz, J.R.C. / Elkins, J. / Wang, J. / Savitzky, P. / Roos, A. / Salah, E. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Weigelt, J. ...Muniz, J.R.C. / Elkins, J. / Wang, J. / Savitzky, P. / Roos, A. / Salah, E. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Weigelt, J. / Bountra, C. / Knapp, S. | ||||||
![]() | ![]() Title: Unusual Binding Interactions in Pdz Domain Crystal Structures Help Explain Binding Mechanisms. Authors: Elkins, J.M. / Gileadi, C. / Shrestha, L. / Phillips, C. / Wang, J. / Muniz, J.R.C. / Doyle, D.A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 87.2 KB | Display | ![]() |
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PDB format | ![]() | 67.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.3 KB | Display | ![]() |
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Full document | ![]() | 430.8 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 14.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2pa1C ![]() 2pktC ![]() 2pntC ![]() 2q3gC ![]() 2uzcC ![]() 2v1wC C: citing same article ( |
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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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.5157, -0.8555, -0.048), Vector: |
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Components
#1: Protein | Mass: 10652.010 Da / Num. of mol.: 2 / Fragment: PDZ DOMAIN, RESIDUES 1143-1234 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: O15021, non-specific serine/threonine protein kinase #2: Chemical | ChemComp-PO4 / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.38 % / Description: NONE |
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Crystal grow | Details: 75MM NA PHOSPHATE, 91MM K PHOSPHATE |
-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 21, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.64→29.14 Å / Num. obs: 32248 / % possible obs: 99.7 % / Observed criterion σ(I): 1.8 / Redundancy: 2.7 % / Biso Wilson estimate: 22.04 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 1.64→1.73 Å / Redundancy: 2.7 % / Mean I/σ(I) obs: 1.8 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 48.11 Å2 / ksol: 0.37 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.6→27.19 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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