1pn7

Coordinates of S12, L11 proteins and P-tRNA, from the 70S X-ray structure aligned to the 70S Cryo-EM map of E.coli ribosome

Method: ELECTRON MICROSCOPY Dmax: 158.2 Å Quality: REASONABLE

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

30S ribosomal protein S12

OrganismNot specified

UniProt Q5SHN3

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 × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain O; UniProt 1–124 Not recorded P-tRNA × 1 50S ribosomal protein L11 × 1 (P29395) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Rapid-freezing in liquid ethane Resolution 10.80 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.

323 other PDB entries and 543 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS12_THET8
Isoform
PDB entities 2
Chains and sequence ranges Author chain O; PDBConstruct 1–124; UniProt 1–124

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–RNA Heteromer Protein × 2 RNA 1 PDB declaration: trimeric(3) Consistent with all polymer counts Chain L; UniProt 7–139 Not recorded P-tRNA × 1 30S ribosomal protein S12 × 1 (Q5SHN3) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Rapid-freezing in liquid ethane Resolution 10.80 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 3
Chains and sequence ranges Author chain L; PDBConstruct 1–133; UniProt 7–139

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 1pn7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pn7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1pn7
Deposition date deposition_date2003-06-12
Structure title titleCoordinates of S12, L11 proteins and P-tRNA, from the 70S X-ray structure aligned to the 70S Cryo-EM map of E.coli ribosome
Keywords keywordsribosomal protein, tRNA binding protein, tRNA, RNA binding protein-RNA COMPLEX; RNA binding protein/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.20
Radius of gyration Rg (electron density) rg_electron45.36
Forward intensity I(0) i017159400.00
Molecular weight molecular_weight29964.0 kDa
Excluded volume excluded_volume35238 ų
Envelope volume envelope_volume67245 ų
Hydration-shell volume shell_volume12686 ų
Envelope diameter envelope_diameter145.0
Shell Rg shell_rg50.51
Envelope Rg envelope_rg41.86
Shape Rg shape_rg46.54
Total Rg total_rg45.59
Total atoms total_atoms62
Residues n_residues62
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 dmax158.2
Rg (real space) rg_real47.15
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real1.7160e+07
I(0) uncertainty (real space) i0_real_error3.2930e+05
Rg (reciprocal space) rg_reciprocal47.19
I(0) (reciprocal space) i0_reciprocal17160000.0000
Solution quality estimate total_estimate0.5934
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary76.7
Skewness Skewness skewness-0.205
Kurtosis Kurtosis kurtosis-0.899
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha975100.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.001; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.709; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1pn7l_
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_idd1pn7o_
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 (1)

9. Files and Curves (10)