3j0d

Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex

Method: ELECTRON MICROSCOPY Dmax: 147.7 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

50S ribosomal protein L11

OrganismNot specified

UniProt P0A7J7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 8 PDB declaration: undecameric(11) Consistent with all polymer counts Chain G; UniProt 2–142 Not recorded ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 16S RNA × 1 ribosomal 16S RNA × 1 30S ribosomal protein S12 × 1 (P0A7S3) Ribosome-recycling factor × 1 (Q9WX76) ELECTRON MICROSCOPY cryo-EM buffer:BUFFER R;pH 7.5;BUFFER R cryo-EM vitrification conditions:Cryogen ETHANE;VITROBOT Resolution 11.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

284 other PDB entries and 329 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL11_ECOLI
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–141; UniProt 2–142

30S ribosomal protein S12

OrganismNot specified

UniProt P0A7S3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 8 PDB declaration: undecameric(11) Consistent with all polymer counts Chain I; UniProt 2–124 Not recorded ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 50S ribosomal protein L11 × 1 (P0A7J7) ribosomal 16S RNA × 1 ribosomal 16S RNA × 1 Ribosome-recycling factor × 1 (Q9WX76) ELECTRON MICROSCOPY cryo-EM buffer:BUFFER R;pH 7.5;BUFFER R cryo-EM vitrification conditions:Cryogen ETHANE;VITROBOT Resolution 11.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

428 other PDB entries and 474 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS12_ECOLI
Isoform
PDB entities 10
Chains and sequence ranges Author chain I; PDBConstruct 1–123; UniProt 2–124

Ribosome-recycling factor

OrganismNot specified

UniProt Q9WX76

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 3 RNA 8 PDB declaration: undecameric(11) Consistent with all polymer counts Chain J; UniProt 1–185 Not recorded ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 ribosomal 23S RNA × 1 50S ribosomal protein L11 × 1 (P0A7J7) ribosomal 16S RNA × 1 ribosomal 16S RNA × 1 30S ribosomal protein S12 × 1 (P0A7S3) ELECTRON MICROSCOPY cryo-EM buffer:BUFFER R;pH 7.5;BUFFER R cryo-EM vitrification conditions:Cryogen ETHANE;VITROBOT Resolution 11.10 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RRF_THET8
Isoform
PDB entities 11
Chains and sequence ranges Author chain J; PDBConstruct 1–185; UniProt 1–185

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3j0d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j0d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j0d
Deposition date deposition_date2011-06-29
Structure title titleModels for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex
Keywords keywordsribosome, ribosome recycling factor, TRANSLATION; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.11
Radius of gyration Rg (electron density) rg_electron44.78
Forward intensity I(0) i0336330000.00
Molecular weight molecular_weight106880.0 kDa
Excluded volume excluded_volume115550 ų
Envelope volume envelope_volume210960 ų
Hydration-shell volume shell_volume41080 ų
Envelope diameter envelope_diameter156.7
Shell Rg shell_rg47.29
Envelope Rg envelope_rg42.94
Shape Rg shape_rg44.71
Total Rg total_rg45.03
Total atoms total_atoms7260
Residues n_residues626
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax147.7
Rg (real space) rg_real45.16
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real3.3630e+08
I(0) uncertainty (real space) i0_real_error5.9860e+06
Rg (reciprocal space) rg_reciprocal45.11
I(0) (reciprocal space) i0_reciprocal336300000.0000
Solution quality estimate total_estimate0.6388
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary38.0
Skewness Skewness skewness0.126
Kurtosis Kurtosis kurtosis-0.887
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7707000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 0.010; Positv: 1.000; Valcen: 0.872; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)