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- PDB-3fe3: Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant -
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Open data
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Basic information
Entry | Database: PDB / ID: 3fe3 | ||||||
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Title | Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant | ||||||
![]() | MAP/microtubule affinity-regulating kinase 3 | ||||||
![]() | TRANSFERASE / SERINE/THREONINE PROTEIN KINASE / MARK / PAR-1 / KIN1 / UBA DOMAIN / C-TAK1 / P78 / MARK3 / ATP-binding / Kinase / Nucleotide-binding / Phosphoprotein / Serine/threonine-protein kinase | ||||||
Function / homology | ![]() peptidyl-serine autophosphorylation / negative regulation of protein localization to nucleus / tau-protein kinase activity / negative regulation of hippo signaling / RAF activation / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / tau protein binding / microtubule cytoskeleton organization / Negative regulation of MAPK pathway ...peptidyl-serine autophosphorylation / negative regulation of protein localization to nucleus / tau-protein kinase activity / negative regulation of hippo signaling / RAF activation / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / tau protein binding / microtubule cytoskeleton organization / Negative regulation of MAPK pathway / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / positive regulation of protein binding / peptidyl-serine phosphorylation / non-specific serine/threonine protein kinase / intracellular signal transduction / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / dendrite / extracellular exosome / ATP binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Nugoor, C. / Marx, A. / Panneerselvam, S. / Mandelkow, E.-M. / Mandelkow, E. | ||||||
![]() | ![]() Title: Crystal structure of the kinase MARK3/Par-1: T211A-S215A double mutant Authors: Nugoor, C. / Marx, A. / Panneerselvam, S. / Mandelkow, E.-M. / Mandelkow, E. #1: ![]() Title: Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1 Authors: Panneerselvam, S. / Marx, A. / Mandelkow, E.-M. / Mandelkow, E. #2: ![]() Title: Structural variations in the catalytic and ubiquitin-associated domains of microtubule-associated protein/microtubule affinity regulating kinase (MARK) 1 and MARK2 Authors: Marx, A. / Nugoor, C. / Muller, J. / Panneerselvam, S. / Timm, T. / Bilang, M. / Mylonas, E. / Svergun, D.I. / Mandelkow, E.-M. / Mandelkow, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 150.1 KB | Display | ![]() |
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PDB format | ![]() | 116.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.7 KB | Display | ![]() |
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Full document | ![]() | 449.1 KB | Display | |
Data in XML | ![]() | 29.5 KB | Display | |
Data in CIF | ![]() | 42.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2hakS 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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Unit cell |
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Details | AUTHOR DETERMINED BIOLOGICAL UNIT: UNKNOWN |
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Components
#1: Protein | Mass: 37619.582 Da / Num. of mol.: 2 Fragment: CATALYTIC AND UBIQUITIN-ASSOCIATED DOMAINS, UNP residues 41-367 Mutation: T211A, S215A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P27448, non-specific serine/threonine protein kinase #2: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE IS BASED ON THE ISOFORM 3 OF DATABASE MARK3_HUMAN. RESIDUES UNP 162-184 ARE MISSING IN ISOFORM 3. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.26 Å3/Da / Density % sol: 62.25 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100mM Hepes, 200mM calcium chloride, 15-18% PEG 3350, 5mM DTT , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MX-225 / Detector: CCD / Date: Jul 13, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→62.3 Å / Num. obs: 75983 / % possible obs: 99.93 % / Redundancy: 4.95 % / Rmerge(I) obs: 0.037 / Net I/σ(I): 20.89 |
Reflection shell | Resolution: 1.9→1.95 Å / Redundancy: 3.71 % / Rmerge(I) obs: 0.405 / Mean I/σ(I) obs: 3.51 / Num. unique all: 5590 / % possible all: 99.6 |
-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2HAK-E (52-304) Resolution: 1.9→51.85 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.943 / WRfactor Rfree: 0.245 / WRfactor Rwork: 0.216 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 5.944 / SU ML: 0.093 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: ISOTROPIC, TLS / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.128 / ESU R Free: 0.125 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES: RESIDUAL ONLY
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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 max: 85.6 Å2 / Biso mean: 38.066 Å2 / Biso min: 20.19 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→51.85 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20
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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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