+
Open data
-
Basic information
Entry | Database: PDB / ID: 1qjb | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | 14-3-3 ZETA/PHOSPHOPEPTIDE COMPLEX (MODE 1) | |||||||||
![]() |
| |||||||||
![]() | KINASE INHIBITOR/PEPTIDE / KINASE INHIBITOR-PEPTIDE COMPLEX / SIGNAL TRANSDUCTION | |||||||||
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 / regulation of synapse maturation / establishment of Golgi localization / 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 / Interleukin-3, Interleukin-5 and GM-CSF signaling / host cell membrane / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / cellular response to glucose starvation / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / 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 / viral process / hippocampal mossy fiber to CA3 synapse / regulation of ERK1 and ERK2 cascade / Deactivation of the beta-catenin transactivating complex / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / Negative regulation of NOTCH4 signaling / lung development / regulation of protein stability / melanosome / angiogenesis / DNA-binding transcription factor binding / vesicle / transmembrane transporter binding / membrane => GO:0016020 / 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 / cytoplasm / cytosol 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. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 114.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 89.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 389.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 409 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 21.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
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: 969.935 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) ![]() #3: Water | ChemComp-HOH / | Sequence details | CHAINS S AND Q ARE DERIVED FROM THE SEQUENCE, VMRSHSYPPT, FOUND IN MOUSE POLYOMAVIRUS (STRAIN 3) ...CHAINS S AND Q ARE DERIVED FROM THE SEQUENCE, VMRSHSYPPT | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 6.2 Details: COMPLEX WAS CRYSTALLIZED FROM 100 MM MES, PH 6.2, 20 MM MGCL2, 20% ISOPROPANOL AND 15% PEG 4000. IMPROVED CRYSTALS BY MICRO- AND MACROSEEDING INTO 100 MM MES, PH 6.2, 20 MM MGCL2, 15-17% ...Details: COMPLEX WAS CRYSTALLIZED FROM 100 MM MES, PH 6.2, 20 MM MGCL2, 20% ISOPROPANOL AND 15% PEG 4000. IMPROVED CRYSTALS BY MICRO- AND MACROSEEDING INTO 100 MM MES, PH 6.2, 20 MM MGCL2, 15-17% ISOPROPANOL A 12% PEG 4000. | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
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: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. obs: 37059 / % possible obs: 83.5 % / Observed criterion σ(I): 2 / Redundancy: 2 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2→2.09 Å / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 2.1 / % possible all: 41.6 |
Reflection shell | *PLUS % possible obs: 41.6 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 FOR CHAINS A AND B WERE NOT SEEN IN THE DENSITY MAPS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→15 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |