+Open data
-Basic information
Entry | Database: PDB / ID: 4beh | |||||||||
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Title | Solution structure of human ribosomal protein P1.P2 heterodimer | |||||||||
Components |
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Keywords | TRANSLATION / STALK / RIBOSOME | |||||||||
Function / homology | Function and homology information cytoplasmic translational elongation / protein kinase activator activity / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / translational elongation / Viral mRNA Translation ...cytoplasmic translational elongation / protein kinase activator activity / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / translational elongation / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / ribonucleoprotein complex binding / cytosolic ribosome / Regulation of expression of SLITs and ROBOs / cytoplasmic translation / cytosolic large ribosomal subunit / structural constituent of ribosome / translation / focal adhesion / extracellular exosome / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | SOLUTION NMR / ARIA | |||||||||
Authors | Lee, K.M. / Yusa, K. / Chu, L.O. / Wing-Heng Yu, C. / Shaw, P.C. / Oono, M. / Miyoshi, T. / Ito, K. / Wong, K.B. / Uchiumi, T. | |||||||||
Citation | Journal: Nucleic Acids Res. / Year: 2013 Title: Solution Structure of Human P1P2 Heterodimer Provides Insights Into the Role of Eukaryotic Stalk in Recruiting the Ribosome-Inactivating Protein Trichosanthin to the Ribosome. Authors: Lee, K.M. / Yusa, K. / Chu, L.O. / Wing-Heng Yu, C. / Oono, M. / Miyoshi, T. / Ito, K. / Shaw, P.C. / Wong, K.B. / Uchiumi, T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4beh.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4beh.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 4beh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4beh_validation.pdf.gz | 577.4 KB | Display | wwPDB validaton report |
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Full document | 4beh_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 4beh_validation.xml.gz | 245.1 KB | Display | |
Data in CIF | 4beh_validation.cif.gz | 222.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/be/4beh ftp://data.pdbj.org/pub/pdb/validation_reports/be/4beh | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11521.863 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41 / References: UniProt: P05386 |
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#2: Protein | Mass: 11747.973 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): C41 / References: UniProt: P05387 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ASYMMETRICALLY LABELED P1.P2 HETERODIMER. C13,N15P1.P2 AND P1.C13,N15P2. |
-Sample preparation
Details | Contents: 10% WATER/90% D2O |
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Sample conditions | Ionic strength: 150 mM / pH: 6.5 / Pressure: 1.0 atm / Temperature: 298.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: ARIA / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION AND LOWEST ENERGY Conformers calculated total number: 100 / Conformers submitted total number: 20 |