+Open data
-Basic information
Entry | Database: PDB / ID: 1a38 | ||||||
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Title | 14-3-3 PROTEIN ZETA BOUND TO R18 PEPTIDE | ||||||
Components |
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Keywords | COMPLEX (SIGNAL TRANSDUCTION/PEPTIDE) / SIGNAL TRANSDUCTION / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) complex | ||||||
Function / homology | Function and homology information 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 / synaptic target recognition / GP1b-IX-V activation signalling / Deactivation of the beta-catenin transactivating complex / respiratory system process ...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 / synaptic target recognition / GP1b-IX-V activation signalling / Deactivation of the beta-catenin transactivating complex / respiratory system process / Rap1 signalling / TP53 Regulates Metabolic Genes / regulation of programmed cell death / Interleukin-3, Interleukin-5 and GM-CSF signaling / tube formation / phosphoserine residue binding / protein targeting / ERK1 and ERK2 cascade / hippocampal mossy fiber to CA3 synapse / regulation of ERK1 and ERK2 cascade / protein sequestering activity / lung development / melanosome / angiogenesis / protein domain specific binding / protein phosphorylation / negative regulation of transcription by RNA polymerase II / signal transduction / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.35 Å | ||||||
Authors | Petosa, C. / Masters, S.C. / Pohl, J. / Wang, B. / Fu, H. / Liddington, R.C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1998 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: Journal: J.Biol.Chem. / Year: 1998 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a38.cif.gz | 89.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a38.ent.gz | 71.3 KB | Display | PDB format |
PDBx/mmJSON format | 1a38.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a3/1a38 ftp://data.pdbj.org/pub/pdb/validation_reports/a3/1a38 | HTTPS FTP |
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-Related structure data
-Links
-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 Source: (gene. exp.) Bos taurus (cattle) / Production host: Escherichia coli (E. coli) / References: UniProt: P63103 #2: Protein/peptide | Mass: 2361.760 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 5.14 Å3/Da / Density % sol: 76.08 % | ||||||||||||||||||||||||||||||||||||
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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: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Oct 1, 1997 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3.35→20 Å / Num. obs: 17105 / % possible obs: 96.7 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Rmerge(I) obs: 0.081 / Rsym value: 0.081 / Net I/σ(I): 18.5 |
Reflection shell | Resolution: 3.35→3.5 Å / Redundancy: 3.15 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 4.9 / Rsym value: 0.32 / % possible all: 91.6 |
Reflection | *PLUS Lowest resolution: 20 Å / Rmerge(I) obs: 0.06 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.35→20 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3.35→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: STRICT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 10 % / Rfactor obs: 0.3 / Rfactor Rfree: 0.35 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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