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Open data
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Basic information
Entry | Database: PDB / ID: 4fzd | ||||||
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Title | Crystal structure of MST4-MO25 complex with WSF motif | ||||||
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![]() | SIGNALING PROTEIN/TRANSFERASE / Scaffold protein / Protein Ser/Thr kinase / ATP binding / SIGNALING PROTEIN-TRANSFERASE complex | ||||||
Function / homology | ![]() negative regulation of potassium ion transmembrane transporter activity / microvillus assembly / negative regulation of potassium ion transmembrane transport / serine/threonine protein kinase complex / cellular hypotonic response / response to thyroid hormone / Energy dependent regulation of mTOR by LKB1-AMPK / vesicle membrane / Golgi-associated vesicle / protein kinase activator activity ...negative regulation of potassium ion transmembrane transporter activity / microvillus assembly / negative regulation of potassium ion transmembrane transport / serine/threonine protein kinase complex / cellular hypotonic response / response to thyroid hormone / Energy dependent regulation of mTOR by LKB1-AMPK / vesicle membrane / Golgi-associated vesicle / protein kinase activator activity / Apoptotic cleavage of cellular proteins / cellular response to starvation / protein serine/threonine kinase activator activity / negative regulation of cell migration / positive regulation of peptidyl-threonine phosphorylation / response to activity / cell periphery / positive regulation of protein serine/threonine kinase activity / kinase binding / Z disc / cellular response to oxidative stress / peptidyl-serine phosphorylation / regulation of apoptotic process / secretory granule lumen / ficolin-1-rich granule lumen / protein autophosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / intracellular signal transduction / apical plasma membrane / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / apoptotic process / Neutrophil degranulation / perinuclear region of cytoplasm / Golgi apparatus / magnesium ion binding / signal transduction / protein homodimerization activity / extracellular exosome / extracellular region / ATP binding / identical protein binding / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Shi, Z.B. / Zhou, Z.C. | ||||||
![]() | ![]() Title: Structure of the MST4 in Complex with MO25 Provides Insights into Its Activation Mechanism Authors: Shi, Z. / Jiao, S. / Zhang, Z. / Ma, M. / Zhang, Z. / Chen, C. / Wang, K. / Wang, H. / Wang, W. / Zhang, L. / Zhao, Y. / Zhou, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 248.1 KB | Display | ![]() |
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PDB format | ![]() | 202.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 455.4 KB | Display | ![]() |
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Full document | ![]() | 464.2 KB | Display | |
Data in XML | ![]() | 22.6 KB | Display | |
Data in CIF | ![]() | 30.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4fzaC ![]() 4fzfC ![]() 1uplS ![]() 3ggfS 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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Unit cell |
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Components
#1: Protein | Mass: 38311.098 Da / Num. of mol.: 1 / Fragment: Mo25-like, UNP residues 11-334 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 31930.670 Da / Num. of mol.: 1 / Fragment: Kinase domain, UNP residues 18-297 / Mutation: D162A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9P289, non-specific serine/threonine protein kinase |
#3: Protein/peptide | Mass: 668.694 Da / Num. of mol.: 1 / Fragment: WSF motif, UNP residues 323-327 / Source method: obtained synthetically / Source: (synth.) ![]() |
#4: Chemical | ChemComp-GOL / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.02 Å3/Da / Density % sol: 69.43 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.1M Tris pH 8.0, 18% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 15, 2012 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97907 Å / Relative weight: 1 |
Reflection | Resolution: 3.25→50 Å / Num. all: 18708 / Num. obs: 18633 / % possible obs: 99.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 6.8 % |
Reflection shell | Resolution: 3.25→3.31 Å / Redundancy: 6.5 % / Mean I/σ(I) obs: 2.9 / Num. unique all: 915 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY: 1UPL and 3GGF Resolution: 3.25→50 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.909 / SU B: 43.597 / SU ML: 0.333 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.441 / 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: 109.175 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.25→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.251→3.335 Å / 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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