+
Open data
-
Basic information
Entry | Database: PDB / ID: 4fza | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of MST4-MO25 complex | ||||||
![]() |
| ||||||
![]() | 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 260.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 214 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 464.6 KB | Display | |
Data in XML | ![]() | 23.5 KB | Display | |
Data in CIF | ![]() | 31.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4fzdC ![]() 4fzfC ![]() 1uplS ![]() 3ggfS C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
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.) ![]() ![]() ![]() | ||
---|---|---|---|
#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: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.98 Å3/Da / Density % sol: 69.08 % |
---|---|
Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.1M Tris pH 8.0, 20% PEG 350 mme, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 11, 2011 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97915 Å / Relative weight: 1 |
Reflection | Resolution: 3.15→50 Å / Num. all: 20053 / Num. obs: 20033 / % possible obs: 99.9 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 3.15→3.2 Å / Redundancy: 19.9 % / Mean I/σ(I) obs: 4 / Num. unique all: 980 / % possible all: 100 |
-
Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY: 1UPL and 3GGF Resolution: 3.15→40.75 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.916 / SU B: 38.699 / SU ML: 0.308 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.413 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 96.584 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.15→40.75 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 3.153→3.235 Å / Total num. of bins used: 20
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group |
|