9qej

Cryo-EM structure of the Importin beta:Importin7:Histone H1.0 complex

Method: ELECTRON MICROSCOPY Dmax: 139.9 Å Quality: GOOD

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

Importin 7 L homeolog

Xenopus laevis

UniProt O42480

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 1–1038 Not recorded Importin subunit beta-1 × 1 (Q14974) Histone H1.0 × 1 (P07305) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O42480_XENLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1038; UniProt 1–1038

Importin subunit beta-1

Homo sapiens

UniProt Q14974

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 1–876 Not recorded Importin 7 L homeolog × 1 (O42480) Histone H1.0 × 1 (P07305) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 Å

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.

22 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–876; UniProt 1–876

Histone H1.0

Homo sapiens

UniProt P07305

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 C; UniProt 1–194 Not recorded Importin 7 L homeolog × 1 (O42480) Importin subunit beta-1 × 1 (Q14974) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.20 Å

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.

15 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H10_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–194; UniProt 1–194

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 9qej

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qej
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qej
Deposition date deposition_date2025-03-10
Structure title titleCryo-EM structure of the Importin beta:Importin7:Histone H1.0 complex
Keywords keywordsTransport, Importin 7, Importin Beta, Histone 1.0, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.02
Radius of gyration Rg (electron density) rg_electron43.49
Forward intensity I(0) i0641478000.00
Molecular weight molecular_weight209620.0 kDa
Excluded volume excluded_volume263170 ų
Envelope volume envelope_volume406600 ų
Hydration-shell volume shell_volume77569 ų
Envelope diameter envelope_diameter139.9
Shell Rg shell_rg49.88
Envelope Rg envelope_rg41.33
Shape Rg shape_rg43.48
Total Rg total_rg43.84
Total atoms total_atoms29372
Residues n_residues1853
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 dmax139.9
Rg (real space) rg_real43.76
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real6.4150e+08
I(0) uncertainty (real space) i0_real_error1.1820e+07
Rg (reciprocal space) rg_reciprocal44.02
I(0) (reciprocal space) i0_reciprocal641700000.0000
Solution quality estimate total_estimate0.8871
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.3
Skewness Skewness skewness0.085
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha73090000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.921

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)