9lj2

Structure of isw1-nucleosome double-bound complex in ADP-ADP+ state

Method: ELECTRON MICROSCOPY Dmax: 183.3 Å Quality: GOOD

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

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 38–135 Chain E; UniProt 38–135 Not recorded Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 ISWI chromatin-remodeling complex ATPase ISW1 × 2 (P38144) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 38–135 Author chain E; PDBConstruct 1–98; UniProt 38–135

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 H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 ISWI chromatin-remodeling complex ATPase ISW1 × 2 (P38144) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 1–88; 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 13–119 Chain G; UniProt 13–119 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 ISWI chromatin-remodeling complex ATPase ISW1 × 2 (P38144) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–107; UniProt 13–119 Author chain G; PDBConstruct 1–107; UniProt 13–119

Histone H2B

Xenopus laevis

UniProt A0A8J0U496

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 33–125 Chain H; UniProt 33–125 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) DNA (147-MER) × 1 DNA (147-MER) × 1 ISWI chromatin-remodeling complex ATPase ISW1 × 2 (P38144) MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J0U496_XENLA
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–93; UniProt 33–125 Author chain H; PDBConstruct 1–93; UniProt 33–125

ISWI chromatin-remodeling complex ATPase ISW1

Saccharomyces cerevisiae S288C

UniProt P38144

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 1–1129 Chain N; UniProt 1–1129 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ISW1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–1129; UniProt 1–1129 Author chain N; PDBConstruct 1–1129; UniProt 1–1129

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 9lj2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lj2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9lj2
Deposition date deposition_date2025-01-14
Structure title titleStructure of isw1-nucleosome double-bound complex in ADP-ADP+ state
Keywords keywordsChromatin Remodeler, Nucleosome, DNA BINDING PROTEIN/DNA, 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_guinier50.45
Radius of gyration Rg (electron density) rg_electron51.62
Forward intensity I(0) i01911520000.00
Molecular weight molecular_weight305460.0 kDa
Excluded volume excluded_volume358100 ų
Envelope volume envelope_volume539370 ų
Hydration-shell volume shell_volume89554 ų
Envelope diameter envelope_diameter185.4
Shell Rg shell_rg53.06
Envelope Rg envelope_rg50.43
Shape Rg shape_rg51.69
Total Rg total_rg51.45
Total atoms total_atoms21131
Residues n_residues2155
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 dmax183.3
Rg (real space) rg_real50.54
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real1.9120e+09
I(0) uncertainty (real space) i0_real_error3.4840e+07
Rg (reciprocal space) rg_reciprocal50.37
I(0) (reciprocal space) i0_reciprocal1911000000.0000
Solution quality estimate total_estimate0.8415
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.1
Skewness Skewness skewness0.466
Kurtosis Kurtosis kurtosis-0.124
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha267000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.693; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)