9gd2

Structure of Chd1 bound to a dinucleosome with a dyad-to-dyad distance of 103 bp.

Method: ELECTRON MICROSCOPY Dmax: 224.6 Å Quality: GOOD

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

Histone H3.2

Xenopus laevis

UniProt P84233

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Chain K; UniProt 1–136 Chain O; UniProt 1–136 Not recorded Histone H4 × 4 (P62799) Histone H2A type 1 × 4 (P06897) Histone H2B 1.1 × 4 (P02281) DNA (248-MER) × 1 DNA (248-MER) × 1 Chromo domain-containing protein 1 × 3 (P32657) ADP ADENOSINE-5'-DIPHOSPHATE × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

230 other PDB entries and 239 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_XENLA
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 Author chain K; PDBConstruct 1–136; UniProt 1–136 Author chain O; 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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Chain L; UniProt 1–103 Chain P; UniProt 1–103 Not recorded Histone H3.2 × 4 (P84233) Histone H2A type 1 × 4 (P06897) Histone H2B 1.1 × 4 (P02281) DNA (248-MER) × 1 DNA (248-MER) × 1 Chromo domain-containing protein 1 × 3 (P32657) ADP ADENOSINE-5'-DIPHOSPHATE × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103 Author chain L; PDBConstruct 1–103; UniProt 1–103 Author chain P; PDBConstruct 1–103; UniProt 1–103

Histone H2A type 1

Xenopus laevis

UniProt P06897

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Chain M; UniProt 1–130 Chain R; UniProt 1–130 Not recorded Histone H3.2 × 4 (P84233) Histone H4 × 4 (P62799) Histone H2B 1.1 × 4 (P02281) DNA (248-MER) × 1 DNA (248-MER) × 1 Chromo domain-containing protein 1 × 3 (P32657) ADP ADENOSINE-5'-DIPHOSPHATE × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

136 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_XENLA
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 Author chain M; PDBConstruct 1–130; UniProt 1–130 Author chain R; PDBConstruct 1–130; UniProt 1–130

Histone H2B 1.1

Xenopus laevis

UniProt P02281

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Chain N; UniProt 5–126 Chain Q; UniProt 5–126 Not recorded Histone H3.2 × 4 (P84233) Histone H4 × 4 (P62799) Histone H2A type 1 × 4 (P06897) DNA (248-MER) × 1 DNA (248-MER) × 1 Chromo domain-containing protein 1 × 3 (P32657) ADP ADENOSINE-5'-DIPHOSPHATE × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

310 other PDB entries and 327 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B11_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–123; UniProt 5–126 Author chain H; PDBConstruct 2–123; UniProt 5–126 Author chain N; PDBConstruct 2–123; UniProt 5–126 Author chain Q; PDBConstruct 2–123; UniProt 5–126

Chromo domain-containing protein 1

Saccharomyces cerevisiae S288C

UniProt P32657

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain S; UniProt 1–1468 Chain T; UniProt 1–1468 Chain W; UniProt 1–1468 Not recorded Histone H3.2 × 4 (P84233) Histone H4 × 4 (P62799) Histone H2A type 1 × 4 (P06897) Histone H2B 1.1 × 4 (P02281) DNA (248-MER) × 1 DNA (248-MER) × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 BEF BERYLLIUM TRIFLUORIDE ION × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHD1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–1468; UniProt 1–1468 Author chain T; PDBConstruct 1–1468; UniProt 1–1468 Author chain W; PDBConstruct 1–1468; UniProt 1–1468

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 9gd2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gd2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gd2
Deposition date deposition_date2024-08-04
Structure title titleStructure of Chd1 bound to a dinucleosome with a dyad-to-dyad distance of 103 bp.
Keywords keywordschromatin, remodeling, transcription, nucleosome, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.71
Radius of gyration Rg (electron density) rg_electron59.50
Forward intensity I(0) i03356140000.00
Molecular weight molecular_weight387280.0 kDa
Excluded volume excluded_volume443790 ų
Envelope volume envelope_volume742150 ų
Hydration-shell volume shell_volume104830 ų
Envelope diameter envelope_diameter210.8
Shell Rg shell_rg61.28
Envelope Rg envelope_rg57.66
Shape Rg shape_rg59.34
Total Rg total_rg59.95
Total atoms total_atoms26638
Residues n_residues2578
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 dmax224.6
Rg (real space) rg_real61.94
Rg uncertainty (real space) rg_real_error2.30
I(0) (real space) i0_real3.3560e+09
I(0) uncertainty (real space) i0_real_error6.9570e+07
Rg (reciprocal space) rg_reciprocal61.49
I(0) (reciprocal space) i0_reciprocal3354000000.0000
Solution quality estimate total_estimate0.8535
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.9
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0008
Highest regularization parameter α highest_alpha221200000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)