8wh5

Structure of DDM1-nucleosome complex in the apo state

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H3.1

Arabidopsis thaliana

UniProt P59226

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H4 × 2 (P59259) Histone H2A.6 × 2 (Q9LD28) Histone H2B.6 × 2 (O23629) DNA (sense strand) × 1 DNA (antisense strand) × 1 ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H31_ARATH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136

Histone H4

Arabidopsis thaliana

UniProt P59259

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3.1 × 2 (P59226) Histone H2A.6 × 2 (Q9LD28) Histone H2B.6 × 2 (O23629) DNA (sense strand) × 1 DNA (antisense strand) × 1 ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H4_ARATH
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Histone H2A.6

Arabidopsis thaliana

UniProt Q9LD28

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Histone H2B.6 × 2 (O23629) DNA (sense strand) × 1 DNA (antisense strand) × 1 ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2A6_ARATH
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–130; UniProt 1–130 Author chain G; PDBConstruct 1–130; UniProt 1–130

Histone H2B.6

Arabidopsis thaliana

UniProt O23629

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Histone H2A.6 × 2 (Q9LD28) DNA (sense strand) × 1 DNA (antisense strand) × 1 ATP-dependent DNA helicase DDM1 × 1 (Q9XFH4) Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name H2B6_ARATH
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–150; UniProt 1–150 Author chain H; PDBConstruct 1–150; UniProt 1–150

ATP-dependent DNA helicase DDM1

Arabidopsis thaliana

UniProt Q9XFH4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–DNA Heteromer Protein 9 DNA 2 Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Histone H2A.6 × 2 (Q9LD28) Histone H2B.6 × 2 (O23629) DNA (sense strand) × 1 DNA (antisense strand) × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DDM1_ARATH
Isoform —
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 2–765; 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id8wh5
Deposition date deposition_date2023-09-22
Structure title titleStructure of DDM1-nucleosome complex in the apo state
Keywords keywordscomplex, nucleosome, chromatin remodeling, structural protein-hydrolase-dna complex, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

8wh5__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8wh5__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8wh5__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)44.35 Å
Rg (electron density)43.17 Å
Total Rg43.57 Å
Atom count14663
Residues1422
Excluded volume245070 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8wh5__assembly_1__model_1 undecameric (11) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (7)

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7. Citations (1)