3uzs

Structure of the C13.28 RNA Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex

Method: X-RAY DIFFRACTION Dmax: 150.2 Å Quality: GOOD

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

Beta-adrenergic receptor kinase 1

Bos taurus

UniProt P21146

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–689 Mutation:S670A Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) C13.28 RNA Aptamer × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris pH 8.5, 200 mM NaCl and 3% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 4.52 Å R-free 0.268

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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARBK1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–681; UniProt 1–689

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Bos taurus

UniProt P62871

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 1–340 Not recorded Beta-adrenergic receptor kinase 1 × 1 (P21146) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) C13.28 RNA Aptamer × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris pH 8.5, 200 mM NaCl and 3% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 4.52 Å R-free 0.268

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.

72 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Bos taurus

UniProt P63212

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 × 3 RNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain G; UniProt 1–67 Non-standard monomer:Yes (specific site not provided by mmCIF) Beta-adrenergic receptor kinase 1 × 1 (P21146) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62871) C13.28 RNA Aptamer × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;277 K;100 mM Tris pH 8.5, 200 mM NaCl and 3% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 4.52 Å R-free 0.268

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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 7–73; UniProt 1–67

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 3uzs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3uzs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3uzs
Deposition date deposition_date2011-12-07
Structure title titleStructure of the C13.28 RNA Aptamer Bound to the G Protein-Coupled Receptor Kinase 2-Heterotrimeric G Protein Beta 1 and Gamma 2 Subunit Complex
Keywords keywords;Protein-RNA complex, Protein Kinase Fold, RGS Homology Domain, Pleckstrin Homology Domain, beta propeller, G Protein-Coupled Receptor Phosphorylation, RNA Aptamer, Carboxymethylation, geranylgeranylation, TRANSFERASE-RNA complex ;; TRANSFERASE/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.18
Radius of gyration Rg (electron density) rg_electron43.51
Forward intensity I(0) i0246961000.00
Molecular weight molecular_weight121970.0 kDa
Excluded volume excluded_volume150070 ų
Envelope volume envelope_volume227370 ų
Hydration-shell volume shell_volume46049 ų
Envelope diameter envelope_diameter154.0
Shell Rg shell_rg44.88
Envelope Rg envelope_rg42.98
Shape Rg shape_rg43.46
Total Rg total_rg43.71
Total atoms total_atoms8535
Residues n_residues1034
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 dmax150.2
Rg (real space) rg_real44.58
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real2.4700e+08
I(0) uncertainty (real space) i0_real_error5.0030e+06
Rg (reciprocal space) rg_reciprocal44.18
I(0) (reciprocal space) i0_reciprocal246800000.0000
Solution quality estimate total_estimate0.8009
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28270000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.714; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.663; Smooth: 0.602

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)