1jqm

Fitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid

Method: ELECTRON MICROSCOPY Dmax: 111.5 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–139 Not recorded Elongation Factor G × 1 (P13551) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–691 Not recorded 50S Ribosomal protein L11 × 1 (P29395) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 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
Chains and sequence ranges Author chain B; PDBConstruct 1–691; UniProt 1–691

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 1jqm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jqm
Deposition date deposition_date2001-08-07
Structure title titleFitting of L11 protein and elongation factor G (EF-G) in the cryo-em map of e. coli 70S ribosome bound with EF-G, GDP and fusidic acid
Keywords keywordsL11, EF-G, cryo-EM, 70s E.coli ribosome, GDP state, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.35
Radius of gyration Rg (electron density) rg_electron36.11
Forward intensity I(0) i0120052000.00
Molecular weight molecular_weight91140.0 kDa
Excluded volume excluded_volume112480 ų
Envelope volume envelope_volume105980 ų
Hydration-shell volume shell_volume26709 ų
Envelope diameter envelope_diameter114.5
Shell Rg shell_rg39.36
Envelope Rg envelope_rg33.59
Shape Rg shape_rg36.14
Total Rg total_rg36.29
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 dmax111.5
Rg (real space) rg_real37.14
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real1.1830e+08
I(0) uncertainty (real space) i0_real_error1.5370e+06
Rg (reciprocal space) rg_reciprocal36.36
I(0) (reciprocal space) i0_reciprocal120100000.0000
Solution quality estimate total_estimate0.6731
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.0
Skewness Skewness skewness0.266
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha3.6950
Highest regularization parameter α highest_alpha7264000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.996; Stabil: 0.902; Sysdev: 0.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.103

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1jqma_
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_idd1jqmb_
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)