7ux9

Arabidopsis DDM1 bound to nucleosome (H2A.W, H2B, H3.3, H4, with 147 bp DNA)

Method: ELECTRON MICROSCOPY Dmax: 151.3 Å Quality: GOOD

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

Probable histone H2A.7

Arabidopsis thaliana

UniProt Q9FJE8

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–150 Chain B; UniProt 1–150 Not recorded Histone H2B × 2 (Q0WT91) Histone H3.3 × 2 (P59169) Histone H4 × 2 (P62799) ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) DNA (sense strand) × 1 DNA (antisense strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 2.5 seconds before plunging. Resolution 3.20 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A7_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–150; UniProt 1–150 Author chain B; PDBConstruct 1–150; UniProt 1–150

Histone H2B

Arabidopsis thaliana

UniProt Q0WT91

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–150 Chain D; UniProt 1–150 Not recorded Probable histone H2A.7 × 2 (Q9FJE8) Histone H3.3 × 2 (P59169) Histone H4 × 2 (P62799) ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) DNA (sense strand) × 1 DNA (antisense strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 2.5 seconds before plunging. Resolution 3.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q0WT91_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–150; UniProt 1–150 Author chain D; PDBConstruct 1–150; UniProt 1–150

Histone H3.3

Arabidopsis thaliana

UniProt P59169

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain E; UniProt 1–136 Chain F; UniProt 1–136 Not recorded Probable histone H2A.7 × 2 (Q9FJE8) Histone H2B × 2 (Q0WT91) Histone H4 × 2 (P62799) ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) DNA (sense strand) × 1 DNA (antisense strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 2.5 seconds before plunging. Resolution 3.20 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_ARATH
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–136; UniProt 1–136 Author chain F; PDBConstruct 1–136; UniProt 1–136

Histone H4

Xenopus laevis

UniProt P62799

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain G; UniProt 1–103 Chain H; UniProt 1–103 Not recorded Probable histone H2A.7 × 2 (Q9FJE8) Histone H2B × 2 (Q0WT91) Histone H3.3 × 2 (P59169) ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) DNA (sense strand) × 1 DNA (antisense strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 2.5 seconds before plunging. Resolution 3.20 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.

354 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–103; UniProt 1–103 Author chain H; PDBConstruct 1–103; UniProt 1–103

ATP-dependent DNA helicase DDM1

Arabidopsis thaliana

UniProt Q9XFH4

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain P; UniProt 1–764 Not recorded Probable histone H2A.7 × 2 (Q9FJE8) Histone H2B × 2 (Q0WT91) Histone H3.3 × 2 (P59169) Histone H4 × 2 (P62799) DNA (sense strand) × 1 DNA (antisense strand) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 2.5 seconds before plunging. Resolution 3.20 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDM1_ARATH
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–764; UniProt 1–764

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 7ux9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ux9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7ux9
Deposition date deposition_date2022-05-05
Structure title titleArabidopsis DDM1 bound to nucleosome (H2A.W, H2B, H3.3, H4, with 147 bp DNA)
Keywords keywordsChromatin remodeler, Helicase, ATPase, Complex, Gene regulation; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.81
Radius of gyration Rg (electron density) rg_electron44.51
Forward intensity I(0) i01163160000.00
Molecular weight molecular_weight225680.0 kDa
Excluded volume excluded_volume259450 ų
Envelope volume envelope_volume423080 ų
Hydration-shell volume shell_volume78751 ų
Envelope diameter envelope_diameter148.3
Shell Rg shell_rg49.80
Envelope Rg envelope_rg43.48
Shape Rg shape_rg44.43
Total Rg total_rg44.91
Total atoms total_atoms15515
Residues n_residues1499
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 dmax151.3
Rg (real space) rg_real45.64
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.1630e+09
I(0) uncertainty (real space) i0_real_error2.1950e+07
Rg (reciprocal space) rg_reciprocal45.81
I(0) (reciprocal space) i0_reciprocal1163000000.0000
Solution quality estimate total_estimate0.8157
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha128600000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)