1qjh

Protein Aggregation and Alzheimer's Disease: Crystallographic Analysis of the Phenomenon. Engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.

Method: X-RAY DIFFRACTION Dmax: 46.1 Å Quality: EXCELLENT

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

30S ribosomal protein S6

Thermus thermophilus

UniProt P23370

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–101 Mutation:YES MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7.00 Resolution 2.20 Å R-free 0.275

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.

51 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS6_THETH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 1–101

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 1qjh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qjh
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1qjh
Deposition date deposition_date1999-06-24
Structure title titleProtein Aggregation and Alzheimer's Disease: Crystallographic Analysis of the Phenomenon. Engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.
Keywords keywordsRIBOSOMAL PROTEIN, ALZHEIMER DISEASE, RIBOSOMAL PROTEIN S6, OLIGOMERIZATION; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.63
Radius of gyration Rg (electron density) rg_electron13.33
Forward intensity I(0) i02441650.00
Molecular weight molecular_weight10954.0 kDa
Excluded volume excluded_volume13825 ų
Envelope volume envelope_volume15735 ų
Hydration-shell volume shell_volume10390 ų
Envelope diameter envelope_diameter44.4
Shell Rg shell_rg18.53
Envelope Rg envelope_rg13.65
Shape Rg shape_rg13.31
Total Rg total_rg14.58
Total atoms total_atoms769
Residues n_residues93
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 dmax46.1
Rg (real space) rg_real14.56
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real2.4420e+06
I(0) uncertainty (real space) i0_real_error2.6950e+04
Rg (reciprocal space) rg_reciprocal14.57
I(0) (reciprocal space) i0_reciprocal2442000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.9
Skewness Skewness skewness0.181
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha417000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qjha_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.14 — Ribosomal protein S6
Family Family familyd.58.14.1 — Ribosomal protein S6

CATH v4.4 (1 domains)

Domain ID domain_id1qjhA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily60 — Ribosomal protein S6/Translation elongation factor EF1B

8. Citations (2)

9. Files and Curves (10)