9n6k

2.88 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 2:1 complex with DNA-binding domain

Method: ELECTRON MICROSCOPY Dmax: 213.7 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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 16–103 Chain F; UniProt 16–103 Not recorded Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3.2 × 2 (P84233) Chromo domain-containing protein 1 × 2 (P32657) DNA Tracking Strand × 1 DNA Lagging Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 1
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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 11–120 Chain G; UniProt 11–120 Not recorded Histone H4 × 2 (P62799) Histone H2B × 2 (A0A8J1LZU9) Histone H3.2 × 2 (P84233) Chromo domain-containing protein 1 × 2 (P32657) DNA Tracking Strand × 1 DNA Lagging Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–110; UniProt 11–120 Author chain G; PDBConstruct 1–110; UniProt 11–120

Histone H2B

Xenopus laevis

UniProt A0A8J1LZU9

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 33–126 Chain H; UniProt 33–126 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H3.2 × 2 (P84233) Chromo domain-containing protein 1 × 2 (P32657) DNA Tracking Strand × 1 DNA Lagging Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 A0A8J1LZU9_XENLA
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–94; UniProt 33–126 Author chain H; PDBConstruct 1–94; UniProt 33–126

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 40–136 Chain E; UniProt 40–136 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Chromo domain-containing protein 1 × 2 (P32657) DNA Tracking Strand × 1 DNA Lagging Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 4
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 40–136 Author chain E; PDBConstruct 1–97; UniProt 40–136

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain K; UniProt 122–1265 Chain L; UniProt 122–1265 Mutation:L886G, L889G, L891G Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J1LZU9) Histone H3.2 × 2 (P84233) DNA Tracking Strand × 1 DNA Lagging Strand × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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 5
Chains and sequence ranges Author chain K; PDBConstruct 1–1144; UniProt 122–1265 Author chain L; PDBConstruct 1–1144; UniProt 122–1265

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 9n6k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n6k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n6k
Deposition date deposition_date2025-02-05
Structure title title2.88 A S.cerevisiae Chd1[L886G/L889G/L891G]-nucleosome 2:1 complex with DNA-binding domain
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_guinier60.13
Radius of gyration Rg (electron density) rg_electron59.94
Forward intensity I(0) i02852590000.00
Molecular weight molecular_weight374120.0 kDa
Excluded volume excluded_volume437600 ų
Envelope volume envelope_volume755130 ų
Hydration-shell volume shell_volume107220 ų
Envelope diameter envelope_diameter234.7
Shell Rg shell_rg58.75
Envelope Rg envelope_rg60.55
Shape Rg shape_rg60.00
Total Rg total_rg59.76
Total atoms total_atoms25954
Residues n_residues2855
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 dmax213.7
Rg (real space) rg_real60.65
Rg uncertainty (real space) rg_real_error2.20
I(0) (real space) i0_real2.8520e+09
I(0) uncertainty (real space) i0_real_error6.4470e+07
Rg (reciprocal space) rg_reciprocal59.66
I(0) (reciprocal space) i0_reciprocal2848000000.0000
Solution quality estimate total_estimate0.8314
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.5
Skewness Skewness skewness0.615
Kurtosis Kurtosis kurtosis0.029
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0006
Highest regularization parameter α highest_alpha245200000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.699; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.705

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)