1jqt

Fitting of L11 protein in the low resolution cryo-EM map of E.coli 70S ribosome

Method: ELECTRON MICROSCOPY Dmax: 58.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–139 Not recorded No other associated polymer 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

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 1jqt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jqt
Deposition date deposition_date2001-08-07
Structure title titleFitting of L11 protein in the low resolution cryo-EM map of E.coli 70S ribosome
Keywords keywordsL11, cryo-EM, 70S E.coli ribosome, RIBOSOME; RIBOSOME
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier18.04
Radius of gyration Rg (electron density) rg_electron17.28
Forward intensity I(0) i03189540.00
Molecular weight molecular_weight14274.0 kDa
Excluded volume excluded_volume17809 ų
Envelope volume envelope_volume12191 ų
Hydration-shell volume shell_volume7102 ų
Envelope diameter envelope_diameter55.1
Shell Rg shell_rg19.79
Envelope Rg envelope_rg15.86
Shape Rg shape_rg17.19
Total Rg total_rg17.62
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 dmax58.2
Rg (real space) rg_real18.07
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.1900e+06
I(0) uncertainty (real space) i0_real_error4.0610e+04
Rg (reciprocal space) rg_reciprocal18.07
I(0) (reciprocal space) i0_reciprocal3190000.0000
Solution quality estimate total_estimate0.8716
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary14.9
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.781
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha527800.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.879; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jqta_
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 (4)

9. Files and Curves (10)