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- PDB-2lbf: Solution structure of the dimerization domain of human ribosomal ... -
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Basic information
Entry | Database: PDB / ID: 2lbf | ||||||
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Title | Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer | ||||||
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![]() | RIBOSOMAL PROTEIN / ribosome / stalk / P1/P2 | ||||||
Function / homology | ![]() cytoplasmic translational elongation / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / protein kinase activator activity / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / translational elongation / Viral mRNA Translation ...cytoplasmic translational elongation / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / protein kinase activator activity / 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 / cytosolic large ribosomal subunit / cytoplasmic translation / structural constituent of ribosome / translation / focal adhesion / extracellular exosome / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | closest to the average, model 1 | ||||||
![]() | Lee, K.-M. / Yu, C.W.-H. / Chiu, T.Y.-H. / Sze, K.-H. / Shaw, P.-C. / Wong, K.-B. | ||||||
![]() | ![]() Title: Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex Authors: Lee, K.-M. / Yu, C.W.-H. / Chiu, T.Y.-H. / Sze, K.-H. / Shaw, P.-C. / Wong, K.-B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 397.4 KB | Display | ![]() |
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PDB format | ![]() | 331 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 547.2 KB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 175.7 KB | Display | |
Data in CIF | ![]() | 166.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 7088.140 Da / Num. of mol.: 1 / Fragment: UNP residues 1-69 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 7207.184 Da / Num. of mol.: 1 / Fragment: UNP residues 1-69 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D 1H-15N ![]() |
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Sample preparation
Details | Contents: 1 mM [U-100% 13C; U-100% 15N] protein_1-1, 1 mM [U-100% 13C; U-100% 15N] protein_2-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 10 / Representative conformer: 3 |