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Open data
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Basic information
Entry | Database: PDB / ID: 5b5w | ||||||
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Title | Crystal structure of MOB1-LATS1 NTR domain complex | ||||||
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![]() | METAL BINDING PROTEIN/APOTOSIS / MOB1 LATS1 Hippo pathway / METAL BINDING PROTEIN-APOTOSIS complex | ||||||
Function / homology | ![]() inner cell mass cell fate commitment / inner cell mass cellular morphogenesis / regulation of protein autophosphorylation / Signaling by Hippo / regulation of ubiquitin-dependent protein catabolic process / sister chromatid segregation / cytoplasmic sequestering of protein / regulation of transforming growth factor beta receptor signaling pathway / hippo signaling / regulation of actin filament polymerization ...inner cell mass cell fate commitment / inner cell mass cellular morphogenesis / regulation of protein autophosphorylation / Signaling by Hippo / regulation of ubiquitin-dependent protein catabolic process / sister chromatid segregation / cytoplasmic sequestering of protein / regulation of transforming growth factor beta receptor signaling pathway / hippo signaling / regulation of actin filament polymerization / mammary gland epithelial cell differentiation / regulation of intracellular estrogen receptor signaling pathway / negative regulation of cyclin-dependent protein serine/threonine kinase activity / regulation of organ growth / kinase activator activity / negative regulation of protein localization to nucleus / Signaling by Hippo / protein kinase activator activity / regulation of protein-containing complex assembly / keratinocyte differentiation / hormone-mediated signaling pathway / nuclear estrogen receptor binding / negative regulation of canonical Wnt signaling pathway / kinase binding / spindle pole / G1/S transition of mitotic cell cycle / G2/M transition of mitotic cell cycle / positive regulation of peptidyl-serine phosphorylation / midbody / non-specific serine/threonine protein kinase / positive regulation of protein phosphorylation / positive regulation of apoptotic process / cell division / protein phosphorylation / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / protein kinase binding / magnesium ion binding / ATP binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | KIM, S.-Y. / Tachioka, Y. / Mori, T. / Hakoshima, T. | ||||||
![]() | ![]() Title: Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway Authors: Kim, S.Y. / Tachioka, Y. / Mori, T. / Hakoshima, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 63.6 KB | Display | ![]() |
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PDB format | ![]() | 44.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.5 KB | Display | ![]() |
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Full document | ![]() | 439.9 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 12.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5b5vC ![]() 5b6bC ![]() 1pi1S 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: 21592.697 Da / Num. of mol.: 1 / Fragment: UNP residues 33-216 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 10379.002 Da / Num. of mol.: 1 / Fragment: UNP residues 622-704 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: O95835, non-specific serine/threonine protein kinase |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.81 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX225HE / Detector: CCD / Date: Nov 26, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.957→30 Å / Num. obs: 6660 / % possible obs: 94.1 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.074 / Net I/σ(I): 21.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1PI1 Resolution: 2.957→28.296 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 37.98
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.957→28.296 Å
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Refine LS restraints |
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LS refinement shell |
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