3ep2

Model of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM

Method: ELECTRON MICROSCOPY Dmax: 151.9 Å Quality: GOOD

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

Elongation factor Tu

OrganismNot specified

UniProt P0A6N1

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 6 PDB declaration: nonameric(9) Consistent with all polymer counts Chain X; UniProt 2–394 Not recorded 30S ribosomal protein S12 × 1 (P0A7S3) 50S ribosomal protein L11 × 1 (P0A7J7) tRNA × 1 Fragment h18 of the 16S rRNA × 1 Fragment h44 of the 16S rRNA × 1 Fragment H43-44 of the 23S rRNA × 1 Fragment H95 of the 23S rRNA × 1 Fragment H69 of the 23S rRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFTU_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–393; UniProt 2–394

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 6 PDB declaration: nonameric(9) Consistent with all polymer counts Chain L; UniProt 2–124 Not recorded Elongation factor Tu × 1 (P0A6N1) 50S ribosomal protein L11 × 1 (P0A7J7) tRNA × 1 Fragment h18 of the 16S rRNA × 1 Fragment h44 of the 16S rRNA × 1 Fragment H43-44 of the 23S rRNA × 1 Fragment H95 of the 23S rRNA × 1 Fragment H69 of the 23S rRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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 2
Chains and sequence ranges Author chain L; PDBConstruct 1–123; UniProt 2–124

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 6 PDB declaration: nonameric(9) Consistent with all polymer counts Chain I; UniProt 2–142 Not recorded Elongation factor Tu × 1 (P0A6N1) 30S ribosomal protein S12 × 1 (P0A7S3) tRNA × 1 Fragment h18 of the 16S rRNA × 1 Fragment h44 of the 16S rRNA × 1 Fragment H43-44 of the 23S rRNA × 1 Fragment H95 of the 23S rRNA × 1 Fragment H69 of the 23S rRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.00 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 3
Chains and sequence ranges Author chain I; PDBConstruct 1–141; UniProt 2–142

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 3ep2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ep2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ep2
Deposition date deposition_date2008-09-29
Structure title titleModel of Phe-tRNA(Phe) in the ribosomal pre-accommodated state revealed by cryo-EM
Keywords keywords;protein translation, ternary complex, A/T-tRNA, automated data collection, Antibiotic resistance, Elongation factor, GTP-binding, Membrane, Methylation, Nucleotide-binding, Phosphoprotein, Protein biosynthesis, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding, RIBOSOMAL PROTEIN-RNA COMPLEX ;; RIBOSOMAL PROTEIN/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.15
Radius of gyration Rg (electron density) rg_electron39.93
Forward intensity I(0) i0130573000.00
Molecular weight molecular_weight77325.0 kDa
Excluded volume excluded_volume89113 ų
Envelope volume envelope_volume146060 ų
Hydration-shell volume shell_volume33089 ų
Envelope diameter envelope_diameter155.0
Shell Rg shell_rg41.30
Envelope Rg envelope_rg39.41
Shape Rg shape_rg41.17
Total Rg total_rg39.98
Total atoms total_atoms187
Residues n_residues187
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 dmax151.9
Rg (real space) rg_real41.24
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real1.3060e+08
I(0) uncertainty (real space) i0_real_error2.5670e+06
Rg (reciprocal space) rg_reciprocal41.15
I(0) (reciprocal space) i0_reciprocal130600000.0000
Solution quality estimate total_estimate0.8573
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary40.0
Skewness Skewness skewness0.320
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha12350000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.910; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (2)

9. Files and Curves (10)