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- PDB-2uv2: Crystal Structure Of Human Ste20-Like Kinase Bound To 4-(4-(5- Cy... -
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Basic information
Entry | Database: PDB / ID: 2uv2 | |||||||||
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Title | Crystal Structure Of Human Ste20-Like Kinase Bound To 4-(4-(5- Cyclopropyl-1H-pyrazol-3-ylamino)-quinazolin-2-ylamino)-phenyl)- acetonitrile | |||||||||
![]() | STE20-LIKE SERINE-THREONINE KINASE | |||||||||
![]() | TRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / PHOSPHORYLATION / MUSCLE DEVELOPMENT / KINASE / APOPTOSIS / GERMINAL CENTRE KINASE / SERINE- THREONINE KINASE 2 / NUCLEOTIDE-BINDING / SERINE-THREONINE-PROTEIN KINASE | |||||||||
Function / homology | ![]() regulation of focal adhesion assembly / RHOB GTPase cycle / RHOC GTPase cycle / cell leading edge / RHOA GTPase cycle / cytoplasmic microtubule organization / regulation of cell migration / regulation of apoptotic process / protein autophosphorylation / non-specific serine/threonine protein kinase ...regulation of focal adhesion assembly / RHOB GTPase cycle / RHOC GTPase cycle / cell leading edge / RHOA GTPase cycle / cytoplasmic microtubule organization / regulation of cell migration / regulation of apoptotic process / protein autophosphorylation / non-specific serine/threonine protein kinase / cadherin binding / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / extracellular exosome / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Pike, A.C.W. / Rellos, P. / Fedorov, O. / Keates, T. / Salah, E. / Savitsky, P. / Papagrigoriou, E. / Bunkoczi, G. / Debreczeni, J.E. / von Delft, F. ...Pike, A.C.W. / Rellos, P. / Fedorov, O. / Keates, T. / Salah, E. / Savitsky, P. / Papagrigoriou, E. / Bunkoczi, G. / Debreczeni, J.E. / von Delft, F. / Arrowsmith, C.H. / Edwards, A. / Weigelt, J. / Sundstrom, M. / Knapp, S. | |||||||||
![]() | ![]() Title: Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites. Authors: Pike, A.C.W. / Rellos, P. / Niesen, F.H. / Turnbull, A. / Oliver, A.W. / Parker, S.A. / Turk, B.E. / Pearl, L.H. / Knapp, S. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.4 KB | Display | ![]() |
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PDB format | ![]() | 57 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 816.4 KB | Display | ![]() |
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Full document | ![]() | 817.3 KB | Display | |
Data in XML | ![]() | 8.7 KB | Display | |
Data in CIF | ![]() | 12.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2j51SC ![]() 2j7tC ![]() 2j90C ![]() 2jflC ![]() 2jfmC S: Starting model for refinement 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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 37162.070 Da / Num. of mol.: 1 / Fragment: KINASE DOMAIN, RESIDUES 19-320 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9H2G2, non-specific serine/threonine protein kinase | ||||||||||
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#2: Chemical | ChemComp-EDO / #3: Chemical | #4: Chemical | ChemComp-GVD / [ | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | K25T MUTATION DUE TO CLONING ARTIFACT | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.53 Å3/Da / Density % sol: 65 % |
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Crystal grow | pH: 6.5 Details: 18% PEG3350, 0.15M POTASSIUM THIOCYANATE, 10% ETHYLENE GLYCOL, 0.1M BISTRISPROPANE PH6.5, pH 6.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 1, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9687 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→60 Å / Num. obs: 24390 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 8.4 % / Biso Wilson estimate: 50 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 14.2 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 6 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 2.1 / % possible all: 95.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2J51 Resolution: 2.3→60 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.931 / SU B: 10.504 / SU ML: 0.141 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.199 / ESU R Free: 0.179 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 44.92 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→60 Å
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Refine LS restraints |
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