9n6h

2.54 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 1:1 complex

Method: ELECTRON MICROSCOPY Dmax: 168.3 Å Quality: GOOD

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

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 B; UniProt 16–103 Chain F; UniProt 16–103 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Chromo domain-containing protein 1 × 1 (P32657) Histone H3 × 2 (A0A310TTQ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–88; UniProt 16–103 Author chain F; PDBConstruct 1–88; UniProt 16–103

Histone H2A

Xenopus laevis

UniProt Q6AZJ8

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 11–120 Chain G; UniProt 11–120 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Chromo domain-containing protein 1 × 1 (P32657) Histone H3 × 2 (A0A310TTQ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

226 other PDB entries and 238 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6AZJ8_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–110; UniProt 11–120 Author chain G; PDBConstruct 1–110; UniProt 11–120

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 33–126 Chain H; UniProt 33–126 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Chromo domain-containing protein 1 × 1 (P32657) Histone H3 × 2 (A0A310TTQ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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 5
Chains and sequence ranges Author chain D; PDBConstruct 1–94; UniProt 33–126 Author chain H; PDBConstruct 1–94; UniProt 33–126

Chromo domain-containing protein 1

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain K; UniProt 122–956 Fragment:residues 122-956 Mutation:L886G, L889G, L891G DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Histone H3 × 2 (A0A310TTQ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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 6
Chains and sequence ranges Author chain K; PDBConstruct 1–835; UniProt 122–956

Histone H3

Xenopus laevis

UniProt A0A310TTQ1

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 39–136 Chain E; UniProt 39–136 Not recorded DNA Tracking Strand × 1 DNA Lagging Strand × 1 Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) Chromo domain-containing protein 1 × 1 (P32657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

126 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A310TTQ1_XENLA
Isoform
PDB entities 7
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 39–136 Author chain E; PDBConstruct 1–98; UniProt 39–136

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 9n6h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n6h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n6h
Deposition date deposition_date2025-02-05
Structure title title2.54 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 1:1 complex
Keywords keywordschromatin, CHD1, remodeler, ATP-dependent chromatin remodeler, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.52
Radius of gyration Rg (electron density) rg_electron47.60
Forward intensity I(0) i01683680000.00
Molecular weight molecular_weight272950.0 kDa
Excluded volume excluded_volume313390 ų
Envelope volume envelope_volume500880 ų
Hydration-shell volume shell_volume86595 ų
Envelope diameter envelope_diameter178.2
Shell Rg shell_rg52.56
Envelope Rg envelope_rg47.28
Shape Rg shape_rg47.50
Total Rg total_rg48.02
Total atoms total_atoms18807
Residues n_residues1873
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 dmax168.3
Rg (real space) rg_real49.49
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real1.6840e+09
I(0) uncertainty (real space) i0_real_error3.3080e+07
Rg (reciprocal space) rg_reciprocal49.52
I(0) (reciprocal space) i0_reciprocal1684000000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.9
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.266
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha147500000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)