SAXSdb — 9qf0

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

Importin 7 L homeolog

Xenopus laevis

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 1–1038	Not recorded	Histone H1.0 × 1 （P07305）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 7.50 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.

Other PDB	Difference from Current Entry 9QF0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6N88 Cryo-EM structure of the Importin7:Importin beta:Histone H1.0 complex Deposited 2018-11-28	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–1038（1038 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.20 Å
9QEJ Cryo-EM structure of the Importin beta:Importin7:Histone H1.0 complex Deposited 2025-03-10	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–1038（1038 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.20 Å

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

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 1–194	Not recorded	Importin 7 L homeolog × 1 （O42480）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 7.50 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.

Other PDB	Difference from Current Entry 9QF0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6HQ1 Solution structure of the globular domain from human histone H1.0 Deposited 2018-09-23	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 24–97（74 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.4；283 K；Ionic strength (raw mmCIF value) 165；Pressure 1 NMR sample composition 0.925 mM [U-99% 13C; U-99% 15N] H1-GD, 10 mM Tris, 157 mM KCl, 0.1 mM EDTA, 0.125 mM DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.25 mM [U-99% 13C; U-99% 15N] H1-GD, 10 mM Tris, 157 mM KCl, 0.1 mM EDTA, 0.125 mM DSS, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6LA2 343 bp di-nucleosome harboring cohesive DNA termini assembled with linker histone H1.0 Deposited 2019-11-11	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 34 PDB declaration: 38-meric	Chain S 1–194（194 aa） Chain T 1–194（194 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291.15 K；Calcium chloride, Potassium chloride, Sodium acetate	Resolution 3.89 Å R-free 0.267
6LA8 349 bp di-nucleosome harboring cohesive DNA termini assembled with linker histone H1.0 Deposited 2019-11-12	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 17 PDB declaration: nonadecameric	Chain S 1–194（194 aa）	Not recorded	CA CALCIUM ION × 23 K POTASSIUM ION × 7	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291.15 K；Calcium chloride, potassium chloride, sodium acetate (cryo-25% MPD)	Resolution 3.40 Å R-free 0.265
6LA9 349 bp di-nucleosome harboring cohesive DNA termini assembled with linker histone H1.0 (high cryoprotectant) Deposited 2019-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: eicosameric	Chain S 1–194（194 aa） Chain T 1–194（194 aa）	Not recorded	CA CALCIUM ION × 40 K POTASSIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291.15 K；Calcium chloride, potassium chloride, sodium acetate	Resolution 3.70 Å R-free 0.266
6LAB 169 bp nucleosome, harboring cohesive DNA termini, assembled with linker histone H1.0 Deposited 2019-11-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: 22-meric	Chain U 1–194（194 aa） Chain V 1–194（194 aa）	Not recorded	CA CALCIUM ION × 20 K POTASSIUM ION × 2 CL CHLORIDE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291.15 K；Calcium chloride, potassium chloride, sodium acetate	Resolution 3.20 Å R-free 0.262
6N88 Cryo-EM structure of the Importin7:Importin beta:Histone H1.0 complex Deposited 2018-11-28	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–194（194 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.20 Å
6N89 Cryo-EM structure of the Importin beta:Histone H1.0 complex Deposited 2018-11-28	Parsed fields agree	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–194（194 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.50 Å
7COW 353 bp di-nucleosome harboring cohesive DNA termini with linker histone H1.0 Deposited 2020-08-05	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 18 PDB declaration: eicosameric	Chain S 2–194（193 aa） Chain T 2–194（193 aa）	Not recorded	CA CALCIUM ION × 3 K POTASSIUM ION × 5 CL CHLORIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；291.15 K；potassium acetate, calcium chloride, potassium chloride	Resolution 2.86 Å R-free 0.297
7DBP Linker histone defines structure and self-association behaviour of the 177 bp human chromosome Deposited 2020-10-21	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 9 PDB declaration: undecameric	Chain K 2–194（193 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
7K5X Cryo-EM structure of a chromatosome containing human linker histone H1.0 Deposited 2020-09-17	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 11 PDB declaration: tridecameric	Chain U 1–194（194 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.93 Å
7XVL Crystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sticky-169an DNA fragment) Deposited 2022-05-24	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 17 PDB declaration: 21-meric	Chain o 2–194（193 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；40-45mM CaCl2, 25mM KCl, 10mM Na-acetate (pH 4.5)	Resolution 3.51 Å R-free 0.280
7XX6 Crystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sticky-169a DNA fragment) Deposited 2022-05-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 17 PDB declaration: 21-meric	Chain o 2–194（193 aa）	Not recorded	CA CALCIUM ION × 21 K POTASSIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；40-45mM CaCl2, 25mM KCl, 10mM Na-acetate (pH 4.5)	Resolution 3.39 Å R-free 0.296
7XX6 Crystal Structure of Nucleosome-H1.0 Linker Histone Assembly (sticky-169a DNA fragment) Deposited 2022-05-28	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 17 PDB declaration: 21-meric	Chain p 2–194（193 aa）	Not recorded	CA CALCIUM ION × 26 K POTASSIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；40-45mM CaCl2, 25mM KCl, 10mM Na-acetate (pH 4.5)	Resolution 3.39 Å R-free 0.296
8TB9 PRC2-J119-450 monomer bound to H1-nucleosome Deposited 2023-06-28	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 15 PDB declaration: heptadecameric	Chain A 1–194（194 aa）	Not recorded	SAH S-ADENOSYL-L-HOMOCYSTEINE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
9IPU cryo-EM structure of the RNF168(1-193)/UbcH5c-Ub ubiquitylation module bound to H1.0-K63-Ub3 modified chromatosome Deposited 2024-07-11	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: tetradecameric	Chain I 1–194（194 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
9QEJ Cryo-EM structure of the Importin beta:Importin7:Histone H1.0 complex Deposited 2025-03-10	Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–194（194 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.20 Å

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	2
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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9qf0
Deposition date deposition_date	2025-03-11
Structure title title	Cryo-EM structure of the mportin7:Histone H1.0 complex
Keywords keywords	Transport, Importin 7, Histone 1.0, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	38.05 Å
Radius of gyration Rg (electron density) rg_electron	37.41 Å
Forward intensity I(0) i0	256924000.00
Molecular weight molecular_weight	130750.0 kDa
Excluded volume excluded_volume	164470 Å³
Envelope volume envelope_volume	241860 Å³
Hydration-shell volume shell_volume	54791 Å³
Envelope diameter envelope_diameter	117.5 Å
Shell Rg shell_rg	43.32 Å
Envelope Rg envelope_rg	35.58 Å
Shape Rg shape_rg	37.42 Å
Total Rg total_rg	37.83 Å
Total atoms total_atoms	18341
Residues n_residues	1142
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	114.5 Å
Rg (real space) rg_real	37.84 Å
Rg uncertainty (real space) rg_real_error	0.62 Å
I(0) (real space) i0_real	2.5690e+08
I(0) uncertainty (real space) i0_real_error	3.9100e+06
Rg (reciprocal space) rg_reciprocal	37.97 Å
I(0) (reciprocal space) i0_reciprocal	257000000.0000
Solution quality estimate total_estimate	0.6828
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	49.1 Å
Skewness Skewness skewness	0.095
Kurtosis Kurtosis kurtosis	-0.647
Angular range angular_range	— – 0.2100 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	41920000.0000
Real-space data points n_real_points	43
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.978; Stabil: 1.000; Sysdev: 0.080; Positv: 1.000; Valcen: 0.993; Smooth: 0.703

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Importin 7 L homeolog
Molecular weight formula_weight	119553.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	18341

MDPNILIEALRGTMDPALREAAERQLNESHKSLHFVSTLLQITMSEQLELPVRQAGVIYLKNMITQYWPDREVTPGELPPHTIPEEDRHCIRENIVEAIMHSPELIRVQLTTCIHHIIKHDYPNRWTAVVEKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLIAAMQHFLPMLKDRYIQLLADPSEQSVLIQKQIFKIFYALVQYTLPLELINQQNLAEWIEILKTVVDRDVPAETLQVDEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNDFAEVFLKAFAVGVQQVLLKVLYQYKEKQYIAPRVLQQTLNYFNQGVSHAVTWKNLKPHIQGIIQDVIFPLMCYTDSDEDLWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTSCSKRKEVLQKTMGFCYQILTEPAADPRKKDGALHMIGSLAEILLKKKIYKDQMEFMLQNHVFPLFSSELGYMRARACWVLHYFCEVKFKVDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYIVPFIRPVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEGSDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAHSLTCQQVSPQMWQLLPLVFDIFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYSMCKKILTGVAGEDAECHAAKLLEVVILQCKGRGIDQVIPLFVEAALERLTREVKTSELRTMCLQVAIAALYYSPPLLFNTLENLRFPNNEEPVTNHFIKQWLNDVDCFLGLHDRKICVLGLCALIELEQRPQVLNQMSSQILPAFLLLFNGLKRAYACHAEQENDSDDDGDGEDDEDAAELGSDEDDIDEEGQEYLEILAKQAGEDGDDEDWEDDDAEETALEGYTTLLDDEDTPIDEYQIFKAIFQKLQGRDPVWYQALTQGLNEDQGKQLQDIATLADQRRAAHESKMIEKHGGYKFNAPVVPSTFNFGNPAPGMN

来源 Source

来源生物 organism	Xenopus laevis
通用名 common_name	African clawed frog
NCBI Class编号 ncbi_taxonomy_id	8355
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Histone H1.0
Molecular weight formula_weight	20927.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	7.500 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	7.50 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	15800

fit	/app/data/saxs_computation/qf/9qf0/9qf0.fit
pddf	/app/data/pr_computation/qf/9qf0/9qf0.pr.out
profile	/app/data/saxs_computation/qf/9qf0/9qf0.dat

Cryo-EM structure of the mportin7:Histone H1.0 complex

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

Importin 7 L homeolog

State in the Current Structure

Other States of the Same Protein in the Database

Histone H1.0

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)