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Open data
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Basic information
Entry | Database: PDB / ID: 1a37 | ||||||
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Title | 14-3-3 PROTEIN ZETA BOUND TO PS-RAF259 PEPTIDE | ||||||
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![]() | COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / ![]() | ||||||
Function / homology | ![]() KSRP (KHSRP) binds and destabilizes mRNA / RHO GTPases activate PKNs / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / NOTCH4 Activation and Transmission of Signal to the Nucleus / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / GP1b-IX-V activation signalling / Deactivation of the beta-catenin transactivating complex / synaptic target recognition / Rap1 signalling ...KSRP (KHSRP) binds and destabilizes mRNA / RHO GTPases activate PKNs / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / NOTCH4 Activation and Transmission of Signal to the Nucleus / Regulation of localization of FOXO transcription factors / Activation of BAD and translocation to mitochondria / GP1b-IX-V activation signalling / Deactivation of the beta-catenin transactivating complex / synaptic target recognition / Rap1 signalling / TP53 Regulates Metabolic Genes / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Petosa, C. / Masters, S.C. / Pohl, J. / Wang, B. / Fu, H. / Liddington, R.C. | ||||||
![]() | ![]() Title: 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. Authors: Petosa, C. / Masters, S.C. / Bankston, L.A. / Pohl, J. / Wang, B. / Fu, H. / Liddington, R.C. #1: ![]() Title: 14-3-3Zeta Binds a Phosphorylated Raf Peptide and an Unphosphorylated Peptide Via its Conserved Amphipathic Groove Authors: Petosa, C. / Masters, S.C. / Bankston, L.A. / Pohl, J. / Wang, B. / Fu, H. / Liddington, R.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.4 KB | Display | ![]() |
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PDB format | ![]() | 65.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 27777.092 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH PHOSPHOSERINE-CONTAINING PEPTIDE DERIVED FROM RAF Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1840.951 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.49 Å3/Da / Density % sol: 77.58 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop / Details: Liu, D., (1995) Nature, 376, 191. | ||||||||||||||||||||||||||||||||||||
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: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.6→20 Å / Num. obs: 14700 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Rsym value: 0.072 / Net I/σ(I): 20 |
Reflection shell | Resolution: 3.6→3.8 Å / Redundancy: 3.7 % / Mean I/σ(I) obs: 7 / Rsym value: 0.258 / % possible all: 98.8 |
Reflection | *PLUS Highest resolution: 3.6 Å / Lowest resolution: 20 Å / Num. obs: 14696 / % possible obs: 99.5 % / Rmerge(I) obs: 0.07 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Refinement step | Cycle: LAST / Resolution: 3.6→20 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / Rfactor obs: 0.31 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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