1jqs

Fitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog

Method: ELECTRON MICROSCOPY Dmax: 89.3 Å Quality: GOOD

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

50S Ribosomal protein L11

OrganismNot specified

UniProt P29395

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–139 Not recorded Elongation Factor G × 1 (P13551) Elongation Factor G × 1 (P13551) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 18.00 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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL11_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–139; UniProt 1–139

Elongation Factor G

OrganismNot specified

UniProt P13551

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 220–251 Chain C; UniProt 606–673 Fragment:;part of domain G' ; Fragment:domain V 50S Ribosomal protein L11 × 1 (P29395) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 18.00 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EFG_THETH
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–32; UniProt 220–251 Author chain C; PDBConstruct 1–68; UniProt 606–673

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 1jqs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jqs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jqs
Deposition date deposition_date2001-08-07
Structure title titleFitting of L11 protein and elongation factor G (domain G' and V) in the cryo-em map of E. coli 70S ribosome bound with EF-G and GMPPCP, a nonhydrolysable GTP analog
Keywords keywordsL11, EF-G, cryo-EM, 70S E.coli ribosome, GTP state, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier27.94
Radius of gyration Rg (electron density) rg_electron27.79
Forward intensity I(0) i010000500.00
Molecular weight molecular_weight25500.0 kDa
Excluded volume excluded_volume31514 ų
Envelope volume envelope_volume27351 ų
Hydration-shell volume shell_volume10463 ų
Envelope diameter envelope_diameter91.0
Shell Rg shell_rg27.84
Envelope Rg envelope_rg26.12
Shape Rg shape_rg27.66
Total Rg total_rg27.80
Total atoms total_atoms
Residues n_residues
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 dmax89.3
Rg (real space) rg_real28.19
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real1.0000e+07
I(0) uncertainty (real space) i0_real_error1.3830e+05
Rg (reciprocal space) rg_reciprocal28.12
I(0) (reciprocal space) i0_reciprocal10000000.0000
Solution quality estimate total_estimate0.8037
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary39.2
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha400300.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.650; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.646; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1jqsa_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.1 — Ribosome complexes
Domain ID domain_idd1jqsb_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.1 — Ribosome complexes
Domain ID domain_idd1jqsc_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.1 — Ribosome complexes

8. Citations (6)

9. Files and Curves (10)