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Open data
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Basic information
Entry | Database: PDB / ID: 5ncm | ||||||
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Title | Crystal structure Cbk1(NTR)-Mob2 complex | ||||||
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![]() | SIGNALING PROTEIN / kinase | ||||||
Function / homology | ![]() regulation of fungal-type cell wall organization / budding cell apical bud growth / cellular bud / prospore membrane / establishment or maintenance of actin cytoskeleton polarity / incipient cellular bud site / cellular bud tip / serine/threonine protein kinase complex / septum digestion after cytokinesis / cellular bud neck ...regulation of fungal-type cell wall organization / budding cell apical bud growth / cellular bud / prospore membrane / establishment or maintenance of actin cytoskeleton polarity / incipient cellular bud site / cellular bud tip / serine/threonine protein kinase complex / septum digestion after cytokinesis / cellular bud neck / mating projection tip / actomyosin structure organization / establishment or maintenance of cell polarity / protein kinase activator activity / regulation of protein secretion / mitotic cytokinesis / cytoplasmic stress granule / actin cytoskeleton / cell cortex / non-specific serine/threonine protein kinase / intracellular signal transduction / positive regulation of protein phosphorylation / cell cycle / phosphorylation / cell division / protein serine kinase activity / protein serine/threonine kinase activity / signal transduction / ATP binding / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gogl, G. / Remenyi, A. / Parker, B. / Weiss, E. | ||||||
![]() | ![]() Title: Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface. Authors: Parker, B.W. / Gogl, G. / Balint, M. / Hetenyi, C. / Remenyi, A. / Weiss, E.L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 128.8 KB | Display | ![]() |
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PDB format | ![]() | 99.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.9 KB | Display | ![]() |
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Full document | ![]() | 442.2 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 14.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nclC ![]() 5ncnC ![]() 5brkS 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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Unit cell |
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Components
#1: Protein | Mass: 28472.338 Da / Num. of mol.: 1 / Fragment: UNP Residues 44-287 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: MOB2, YFL034C-B, YFL035C, YFL035C-A / Production host: ![]() ![]() |
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#2: Protein | Mass: 12209.621 Da / Num. of mol.: 1 / Fragment: UNP Residues 251-351 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: CBK1, YNL161W, N1727 / Production host: ![]() ![]() References: UniProt: P53894, non-specific serine/threonine protein kinase |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 51.03 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop Details: 100mM MES/Imidazole, 30mM CaCl 2 , 30mM MgCl 2 , 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350, 12.5% (v/v) MPD PH range: 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 24, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→39.93 Å / Num. obs: 10323 / % possible obs: 99.8 % / Redundancy: 14 % / CC1/2: 1 / Rmerge(I) obs: 0.1 / Net I/σ(I): 21.8 |
Reflection shell | Resolution: 2.8→2.87 Å / Redundancy: 14.7 % / Rmerge(I) obs: 1.52 / Mean I/σ(I) obs: 2.21 / Num. unique obs: 750 / CC1/2: 0.67 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5BRK Resolution: 2.8→39.93 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 29.61
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→39.93 Å
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Refine LS restraints |
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LS refinement shell |
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