4toi

Crystal structure of E.coli ribosomal protein S2 in complex with N-terminal domain of S1

Method: X-RAY DIFFRACTION Dmax: 91.7 Å Quality: REASONABLE

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

30S ribosomal protein S2,Ribosomal protein S1

Escherichia coli TA206

UniProt C3TPN2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: Dimeric(2) Consistent with protein copy count Chain A; UniProt 1–236 Fragment:1-236,3-84 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;295.15 K;0.1 M HEPES-KOH, pH 7.4, 3 mM MgCl2, 7.5% w/v PEG 6000, 3% w/v 2-methyl-pentanediol-2,4, 100 mM KCl Resolution 2.30 Å R-free 0.229

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.

104 other PDB entries and 104 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C3TPN2_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–239; UniProt 1–236

30S ribosomal protein S2,Ribosomal protein S1

Escherichia coli TA206

UniProt F4TQ64

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: Dimeric(2) Consistent with protein copy count Chain A; UniProt 3–84 Fragment:1-236,3-84 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;295.15 K;0.1 M HEPES-KOH, pH 7.4, 3 mM MgCl2, 7.5% w/v PEG 6000, 3% w/v 2-methyl-pentanediol-2,4, 100 mM KCl Resolution 2.30 Å R-free 0.229

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name F4TQ64_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 245–326; UniProt 3–84

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 4toi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4toi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4toi
Deposition date deposition_date2014-06-05
Structure title titleCrystal structure of E.coli ribosomal protein S2 in complex with N-terminal domain of S1
Keywords keywordsribosomal protein, complex, translation; RIBOSOMAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.20
Radius of gyration Rg (electron density) rg_electron27.96
Forward intensity I(0) i019878300.00
Molecular weight molecular_weight33794.0 kDa
Excluded volume excluded_volume42309 ų
Envelope volume envelope_volume63263 ų
Hydration-shell volume shell_volume20756 ų
Envelope diameter envelope_diameter94.8
Shell Rg shell_rg32.16
Envelope Rg envelope_rg28.74
Shape Rg shape_rg27.97
Total Rg total_rg28.48
Total atoms total_atoms2376
Residues n_residues307
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 dmax91.7
Rg (real space) rg_real28.42
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real1.9880e+07
I(0) uncertainty (real space) i0_real_error3.4690e+05
Rg (reciprocal space) rg_reciprocal28.36
I(0) (reciprocal space) i0_reciprocal19880000.0000
Solution quality estimate total_estimate0.6819
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.697
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1773000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.695; Smooth: 0.846

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4toiA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10490 — Glucose-6-phosphate isomerase like protein; domain 1
Domain ID domain_id4toiA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily610 — Helix hairpin bin

8. Citations (1)

9. Files and Curves (10)