8q8k

KI Polyomavirus LTA NLS bound to importin alpha 2

Method: X-RAY DIFFRACTION Dmax: 154.7 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 70–529 Not recorded Large T antigen × 1 (P0DOI6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.2 M NaCl, 0.1 M Tris pH 8.0, 16 % PEG4000. Protein stock pre-treated with 5:1 molar ratio IMPa: ivermectin Resolution 2.70 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 70–529 Not recorded Large T antigen × 1 (P0DOI6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.2 M NaCl, 0.1 M Tris pH 8.0, 16 % PEG4000. Protein stock pre-treated with 5:1 molar ratio IMPa: ivermectin Resolution 2.70 Å R-free 0.247

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 150 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 Author chain B; PDBConstruct 51–510; UniProt 70–529

Large T antigen

OrganismNot specified

UniProt P0DOI6

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 119–140 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.2 M NaCl, 0.1 M Tris pH 8.0, 16 % PEG4000. Protein stock pre-treated with 5:1 molar ratio IMPa: ivermectin Resolution 2.70 Å R-free 0.247
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 119–140 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.2 M NaCl, 0.1 M Tris pH 8.0, 16 % PEG4000. Protein stock pre-treated with 5:1 molar ratio IMPa: ivermectin Resolution 2.70 Å R-free 0.247

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 LT_POVK6
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–22; UniProt 119–140 Author chain D; PDBConstruct 1–22; UniProt 119–140

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 8q8k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q8k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q8k
Deposition date deposition_date2023-08-18
Structure title titleKI Polyomavirus LTA NLS bound to importin alpha 2
Keywords keywordsimportin, karyopherin, nuclear, nls, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.10
Radius of gyration Rg (electron density) rg_electron41.45
Forward intensity I(0) i0119872000.00
Molecular weight molecular_weight90173.0 kDa
Excluded volume excluded_volume113760 ų
Envelope volume envelope_volume150160 ų
Hydration-shell volume shell_volume35500 ų
Envelope diameter envelope_diameter153.1
Shell Rg shell_rg38.99
Envelope Rg envelope_rg41.66
Shape Rg shape_rg41.45
Total Rg total_rg41.27
Total atoms total_atoms12668
Residues n_residues868
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 dmax154.7
Rg (real space) rg_real41.77
Rg uncertainty (real space) rg_real_error2.44
I(0) (real space) i0_real1.1990e+08
I(0) uncertainty (real space) i0_real_error2.4400e+06
Rg (reciprocal space) rg_reciprocal41.11
I(0) (reciprocal space) i0_reciprocal119800000.0000
Solution quality estimate total_estimate0.7110
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.675
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9777000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.373; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.289; Smooth: 0.830

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)