23qh

Structure of importin alpha bound to the Psittacine Adenovirus B Fiber 1 protein nuclear localization signal

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 E; UniProt 70–529 Not recorded Peptide from Fiber 1 protein × 2 (A0AB38ZPD2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.6 M sodium citrate, 0.1 M HEPES Resolution 2.10 Å R-free 0.215

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 E; PDBConstruct 51–510; UniProt 70–529

Peptide from Fiber 1 protein

OrganismNot specified

UniProt A0AB38ZPD2

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 23–49 Chain C; UniProt 23–49 Not recorded Importin subunit alpha-1 × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;296 K;0.6 M sodium citrate, 0.1 M HEPES Resolution 2.10 Å R-free 0.215

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 A0AB38ZPD2_9ADEN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–27; UniProt 23–49 Author chain C; PDBConstruct 1–27; UniProt 23–49

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 23qh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 23qh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id23qh
Deposition date deposition_date2026-02-13
最后修订 last_revision2026-03-25
Structure title titleStructure of importin alpha bound to the Psittacine Adenovirus B Fiber 1 protein nuclear localization signal
Keywords keywordsimportin, karyopherin, adenovirus, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.34
Radius of gyration Rg (electron density) rg_electron28.10
Forward intensity I(0) i035026800.00
Molecular weight molecular_weight47655.0 kDa
Excluded volume excluded_volume60362 ų
Envelope volume envelope_volume73168 ų
Hydration-shell volume shell_volume23353 ų
Envelope diameter envelope_diameter102.4
Shell Rg shell_rg33.09
Envelope Rg envelope_rg28.17
Shape Rg shape_rg28.11
Total Rg total_rg28.60
Total atoms total_atoms6811
Residues n_residues438
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_real28.71
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real3.5030e+07
I(0) uncertainty (real space) i0_real_error5.3000e+05
Rg (reciprocal space) rg_reciprocal28.60
I(0) (reciprocal space) i0_reciprocal35020000.0000
Solution quality estimate total_estimate0.7836
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.537
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14520000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.642; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.497; Smooth: 0.759

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)