8u36

The crystal structure of the classical binding interface of Importin alpha 2 and a nuclear localisation signal sequence in Frog siadenovirus core protein VII

Method: X-RAY DIFFRACTION Dmax: 98.9 Å Quality: GOOD

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

Importin subunit alpha-1

Mus musculus

UniProt P52293

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–529 Fragment:UNP residues 70-529 PVII × 2 (Q9IIH8) NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;296 K;0.65 M sodium citrate, 0.1 M sodium HEPES, 1% dithiothreitol Resolution 2.60 Å R-free 0.242

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 51–510; UniProt 70–529

PVII

OrganismNot specified

UniProt Q9IIH8

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 141–149 Chain C; UniProt 141–149 Fragment:UNP residues 141-149 Importin subunit alpha-1 × 1 (P52293) NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;296 K;0.65 M sodium citrate, 0.1 M sodium HEPES, 1% dithiothreitol Resolution 2.60 Å R-free 0.242

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 Q9IIH8_ADEF1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–9; UniProt 141–149 Author chain C; PDBConstruct 1–9; UniProt 141–149

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 8u36

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u36
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u36
Deposition date deposition_date2023-09-07
Structure title titleThe crystal structure of the classical binding interface of Importin alpha 2 and a nuclear localisation signal sequence in Frog siadenovirus core protein VII
Keywords keywordsAdenovirus protein VII, Nuclear localization, Importin alpha, DNA virus, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.06
Radius of gyration Rg (electron density) rg_electron27.91
Forward intensity I(0) i033804200.00
Molecular weight molecular_weight46824.0 kDa
Excluded volume excluded_volume59321 ų
Envelope volume envelope_volume71616 ų
Hydration-shell volume shell_volume22994 ų
Envelope diameter envelope_diameter102.6
Shell Rg shell_rg33.00
Envelope Rg envelope_rg28.01
Shape Rg shape_rg27.90
Total Rg total_rg28.44
Total atoms total_atoms6655
Residues n_residues434
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 dmax98.9
Rg (real space) rg_real28.42
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real3.3800e+07
I(0) uncertainty (real space) i0_real_error4.7450e+05
Rg (reciprocal space) rg_reciprocal28.32
I(0) (reciprocal space) i0_reciprocal33800000.0000
Solution quality estimate total_estimate0.7897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.543
Kurtosis Kurtosis kurtosis-0.391
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13530000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.617; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.515; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)