8tur

Merkel Cell Polyomavirus LTA bipartite NLS bound to importin alpha 2

Method: X-RAY DIFFRACTION Dmax: 98.9 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 Truncated large T antigen × 1 (M4VRX3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.65 M sodium citrate, 0.1 M HEPES pH 6.5, 0.01 M DTT Resolution 2.15 Å R-free 0.208

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

Truncated large T antigen

OrganismNot specified

UniProt M4VRX3

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 B; UniProt 274–308 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.65 M sodium citrate, 0.1 M HEPES pH 6.5, 0.01 M DTT Resolution 2.15 Å R-free 0.208

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 M4VRX3_9POLY
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–35; UniProt 274–308

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 8tur

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tur
Deposition date deposition_date2023-08-17
Structure title titleMerkel Cell Polyomavirus LTA bipartite NLS bound to importin alpha 2
Keywords keywordsimportin, karyopherin, nuclear, nls, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.14
Radius of gyration Rg (electron density) rg_electron27.88
Forward intensity I(0) i035962700.00
Molecular weight molecular_weight48151.0 kDa
Excluded volume excluded_volume60969 ų
Envelope volume envelope_volume74004 ų
Hydration-shell volume shell_volume23861 ų
Envelope diameter envelope_diameter102.2
Shell Rg shell_rg32.83
Envelope Rg envelope_rg27.96
Shape Rg shape_rg27.87
Total Rg total_rg28.39
Total atoms total_atoms6872
Residues n_residues443
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_real28.50
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real3.5960e+07
I(0) uncertainty (real space) i0_real_error5.9430e+05
Rg (reciprocal space) rg_reciprocal28.39
I(0) (reciprocal space) i0_reciprocal35960000.0000
Solution quality estimate total_estimate0.7201
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.543
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16320000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.620; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.506; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)