3deg

Complex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP

Method: ELECTRON MICROSCOPY Dmax: 158.6 Å Quality: GOOD

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

GTP-binding protein lepA

Escherichia coli

UniProt P60785

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 C; UniProt 1–545 Fragment:EF4 A/L-tRNA × 1 P-tRNA × 1 30S RNA helix 8 × 1 30S RNA helix 14 × 1 50S RNA helix 42-44 × 1 50S RNA helix 95 × 1 50S RNA helix 71 × 1 50S RNA helix 92 × 1 30S ribosomal protein S12 × 1 (P0A7S3) 50S ribosomal protein L11 × 1 (P0A7J7) ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES-KOH (pH 7.6), 4.5 mM Mg(CH3COO)2, 150 mM NH4CH3COO, 4 mM B-mercaptoethanol, 2 mM spermidine, and 0.05 mM spermine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.90 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.

3 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEPA_ECOLI
Isoform
PDB entities 9
Chains and sequence ranges Author chain C; PDBConstruct 1–545; UniProt 1–545

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 D; UniProt 2–124 Not recorded A/L-tRNA × 1 P-tRNA × 1 30S RNA helix 8 × 1 30S RNA helix 14 × 1 50S RNA helix 42-44 × 1 50S RNA helix 95 × 1 50S RNA helix 71 × 1 50S RNA helix 92 × 1 GTP-binding protein lepA × 1 (P60785) 50S ribosomal protein L11 × 1 (P0A7J7) ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES-KOH (pH 7.6), 4.5 mM Mg(CH3COO)2, 150 mM NH4CH3COO, 4 mM B-mercaptoethanol, 2 mM spermidine, and 0.05 mM spermine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.90 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 D; 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 8 PDB declaration: undecameric(11) Consistent with all polymer counts Chain H; UniProt 2–142 Not recorded A/L-tRNA × 1 P-tRNA × 1 30S RNA helix 8 × 1 30S RNA helix 14 × 1 50S RNA helix 42-44 × 1 50S RNA helix 95 × 1 50S RNA helix 71 × 1 50S RNA helix 92 × 1 GTP-binding protein lepA × 1 (P60785) 30S ribosomal protein S12 × 1 (P0A7S3) ELECTRON MICROSCOPY cryo-EM buffer:20 mM HEPES-KOH (pH 7.6), 4.5 mM Mg(CH3COO)2, 150 mM NH4CH3COO, 4 mM B-mercaptoethanol, 2 mM spermidine, and 0.05 mM spermine cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.90 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 11
Chains and sequence ranges Author chain H; 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 3deg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3deg
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3deg
Deposition date deposition_date2008-06-10
Structure title titleComplex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP
Keywords keywords;ribosome, translation, LepA, EF4, GTP-binding, Membrane, Nucleotide-binding, Antibiotic resistance, Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding, Methylation ;; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.92
Radius of gyration Rg (electron density) rg_electron46.51
Forward intensity I(0) i01044470000.00
Molecular weight molecular_weight190660.0 kDa
Excluded volume excluded_volume206490 ų
Envelope volume envelope_volume366270 ų
Hydration-shell volume shell_volume66850 ų
Envelope diameter envelope_diameter166.8
Shell Rg shell_rg50.15
Envelope Rg envelope_rg45.55
Shape Rg shape_rg46.40
Total Rg total_rg46.86
Total atoms total_atoms12950
Residues n_residues1106
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 dmax158.6
Rg (real space) rg_real47.81
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real1.0440e+09
I(0) uncertainty (real space) i0_real_error1.9190e+07
Rg (reciprocal space) rg_reciprocal47.92
I(0) (reciprocal space) i0_reciprocal1045000000.0000
Solution quality estimate total_estimate0.8888
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.357
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22250000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3degd1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.5 — Cold shock DNA-binding domain-like
Domain ID domain_idd3degh1
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.7 — Ribosomal protein L11, C-terminal domain
Family Family familya.4.7.1 — Ribosomal protein L11, C-terminal domain
Domain ID domain_idd3degh2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.47 — Ribosomal L11/L12e N-terminal domain
Superfamily Superfamily superfamilyd.47.1 — Ribosomal L11/L12e N-terminal domain
Family Family familyd.47.1.1 — Ribosomal L11/L12e N-terminal domain

8. Citations (1)

9. Files and Curves (10)