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Open data
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Basic information
Entry | Database: PDB / ID: 4fie | ||||||
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Title | Full-length human PAK4 | ||||||
![]() | Serine/threonine-protein kinase PAK 4 | ||||||
![]() | TRANSFERASE / Serine/Threonine-protein kinase PAK4 / Kinase domain / Protein kinase / ATP binding / Phosphorylation | ||||||
Function / homology | ![]() dendritic spine development / cadherin binding involved in cell-cell adhesion / Activation of RAC1 / RHOV GTPase cycle / RHOJ GTPase cycle / RHOQ GTPase cycle / regulation of MAPK cascade / CDC42 GTPase cycle / RHOH GTPase cycle / RHOU GTPase cycle ...dendritic spine development / cadherin binding involved in cell-cell adhesion / Activation of RAC1 / RHOV GTPase cycle / RHOJ GTPase cycle / RHOQ GTPase cycle / regulation of MAPK cascade / CDC42 GTPase cycle / RHOH GTPase cycle / RHOU GTPase cycle / cellular response to organic cyclic compound / RHOG GTPase cycle / RAC2 GTPase cycle / RAC3 GTPase cycle / negative regulation of endothelial cell apoptotic process / cytoskeleton organization / RAC1 GTPase cycle / regulation of cell growth / adherens junction / positive regulation of angiogenesis / cell migration / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / cell cycle / phosphorylation / protein serine kinase activity / focal adhesion / protein serine/threonine kinase activity / apoptotic process / Golgi apparatus / signal transduction / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ha, B.H. / Boggon, T.J. | ||||||
![]() | ![]() Title: Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Authors: Ha, B.H. / Davis, M.J. / Chen, C. / Lou, H.J. / Gao, J. / Zhang, R. / Krauthammer, M. / Halaban, R. / Schlessinger, J. / Turk, B.E. / Boggon, T.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 | ![]() | 137 KB | Display | ![]() |
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PDB format | ![]() | 103.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 30.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4fifC ![]() 4figC ![]() 4fihC ![]() 4fiiC ![]() 4fijC ![]() 2cdzS C: citing same article ( S: Starting model for refinement |
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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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 47668.883 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: O96013, non-specific serine/threonine protein kinase #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | SEQUENCE CORRESPONDS TO ISOFORM 2 OF SERINE/THREONINE-PROTEIN KINASE PAK 4, UNP ACCESSION CODE ...SEQUENCE CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.75 Å3/Da / Density % sol: 67.24 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.1M HEPES, 500 mM K/Na tartrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 30, 2011 / Details: insertion device |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / % possible obs: 96.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6.6 % / Biso Wilson estimate: 101.4 Å2 / Rmerge(I) obs: 0.154 / Rsym value: 0.154 / Net I/σ(I): 11.16 |
Reflection shell | Resolution: 3.1→3.21 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0 / Mean I/σ(I) obs: 1.2 / Rsym value: 0 / % possible all: 83.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2CDZ Resolution: 3.11→46.5 Å / Cor.coef. Fo:Fc: 0.919 / Cor.coef. Fo:Fc free: 0.915 / SU B: 21.361 / SU ML: 0.346 / Cross valid method: THROUGHOUT / ESU R: 0.971 / ESU R Free: 0.407 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 93.29 Å2
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Refinement step | Cycle: LAST / Resolution: 3.11→46.5 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.106→3.186 Å / Total num. of bins used: 20
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