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Open data
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Basic information
Entry | Database: PDB / ID: 1qja | ||||||
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Title | 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 2) | ||||||
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![]() | KINASE INHIBITOR/PEPTIDE / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / COMPLEX / 14-3-3 / PHOSPHOPEPTIDE / SIGNAL TRANSDUCTION / KINASE INHIBITOR-PEPTIDE complex | ||||||
Function / homology | ![]() KSRP (KHSRP) binds and destabilizes mRNA / NOTCH4 Activation and Transmission of Signal to the Nucleus / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / protein localization => GO:0008104 / Golgi reassembly / synaptic target recognition / Rap1 signalling / TP53 Regulates Metabolic Genes / Interleukin-3, Interleukin-5 and GM-CSF signaling ...KSRP (KHSRP) binds and destabilizes mRNA / NOTCH4 Activation and Transmission of Signal to the Nucleus / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / protein localization => GO:0008104 / Golgi reassembly / synaptic target recognition / Rap1 signalling / TP53 Regulates Metabolic Genes / Interleukin-3, Interleukin-5 and GM-CSF signaling / respiratory system process / NOTCH4 Activation and Transmission of Signal to the Nucleus / establishment of Golgi localization / regulation of synapse maturation / tube formation / Rap1 signalling / negative regulation of protein localization to nucleus / KSRP (KHSRP) binds and destabilizes mRNA / GP1b-IX-V activation signalling / Regulation of localization of FOXO transcription factors / phosphoserine residue binding / Interleukin-3, Interleukin-5 and GM-CSF signaling / Activation of BAD and translocation to mitochondria / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / cellular response to glucose starvation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / negative regulation of TORC1 signaling / protein sequestering activity / ERK1 and ERK2 cascade / negative regulation of innate immune response / hippocampal mossy fiber to CA3 synapse / regulation of ERK1 and ERK2 cascade / Translocation of SLC2A4 (GLUT4) to the plasma membrane / Deactivation of the beta-catenin transactivating complex / TP53 Regulates Metabolic Genes / Negative regulation of NOTCH4 signaling / lung development / regulation of protein stability / protein localization / melanosome / angiogenesis / DNA-binding transcription factor binding / vesicle / transmembrane transporter binding / blood microparticle / cadherin binding / protein domain specific binding / protein phosphorylation / focal adhesion / glutamatergic synapse / ubiquitin protein ligase binding / negative regulation of apoptotic process / protein kinase binding / negative regulation of transcription by RNA polymerase II / signal transduction / RNA binding / extracellular space / extracellular exosome / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rittinger, K. / Budman, J. / Xu, J. / Volinia, S. / Cantley, L.C. / Smerdon, S.J. / Gamblin, S.J. / Yaffe, M.B. | ||||||
![]() | ![]() Title: Structural Analysis of 14-3-3 Phosphopeptide Complexes Identifies a Dual Role for the Nuclear Export Signal of 14-3-3 in Ligand Binding Authors: Rittinger, K. / Budman, J. / Xu, J. / Volinia, S. / Cantley, L.C. / Smerdon, S.J. / Gamblin, S.J. / Yaffe, M.B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 107.6 KB | Display | ![]() |
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PDB format | ![]() | 84.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 27777.092 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1038.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Water | ChemComp-HOH / | Sequence details | THE PEPTIDES Q AND R WERE FOUND IN A PEPTIDE LIBRARY SCREEN. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.2 Details: COMPLEX WAS CRYSTALLIZED FROM 100 MM PIPES, PH 6.2, 20 MM MGCL2, 20% ISOPROPANOL AND 15% PEG 4000. IMPROVED CRYSTALS BY MICRO- AND MACROSEEDING INTO 100 MM PIPES, PH 6.2, 20 MM MGCL2, 15-17% ...Details: COMPLEX WAS CRYSTALLIZED FROM 100 MM PIPES, PH 6.2, 20 MM MGCL2, 20% ISOPROPANOL AND 15% PEG 4000. IMPROVED CRYSTALS BY MICRO- AND MACROSEEDING INTO 100 MM PIPES, PH 6.2, 20 MM MGCL2, 15-17% ISOPROPANOL AND 12% PEG 4000. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Details: MIRROR |
Radiation | Monochromator: SINGLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. obs: 41523 / % possible obs: 95.2 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 18.5 |
Reflection shell | Resolution: 2→2.09 Å / Rmerge(I) obs: 0.269 / Mean I/σ(I) obs: 3.9 / % possible all: 94.4 |
Reflection shell | *PLUS % possible obs: 94.4 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 14-3-3 ZETA Resolution: 2→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: THE C-TERMINAL RESIDUES WERE NOT SEEN IN THE DESITY MAPS FOR BOTH CHAINS A AND B
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Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.214 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |