9t4v

ALC1/CHD1L in an intermediate conformation, bound to a PARylated nucleosome

Method: ELECTRON MICROSCOPY Dmax: 174.9 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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence × 1 Widom 601 sequence × 1 Chromodomain-helicase-DNA-binding protein 1-like × 1 (Q86WJ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL were applied on grid and immediately blotted for 2.5 s at blot force 0. Resolution 6.60 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 2–136; UniProt 2–136 Author chain E; PDBConstruct 2–136; UniProt 2–136

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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.2 × 2 (P84233) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence × 1 Widom 601 sequence × 1 Chromodomain-helicase-DNA-binding protein 1-like × 1 (Q86WJ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL were applied on grid and immediately blotted for 2.5 s at blot force 0. Resolution 6.60 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

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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence × 1 Widom 601 sequence × 1 Chromodomain-helicase-DNA-binding protein 1-like × 1 (Q86WJ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL were applied on grid and immediately blotted for 2.5 s at blot force 0. Resolution 6.60 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

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: 11-meric(11) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Widom 601 sequence × 1 Widom 601 sequence × 1 Chromodomain-helicase-DNA-binding protein 1-like × 1 (Q86WJ1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL were applied on grid and immediately blotted for 2.5 s at blot force 0. Resolution 6.60 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

Chromodomain-helicase-DNA-binding protein 1-like

Homo sapiens

UniProt Q86WJ1

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: 11-meric(11) Consistent with all polymer counts Chain K; UniProt 16–879 Not recorded Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A type 1 × 2 (P06897) Histone H2B 1.1 × 2 (P02281) Widom 601 sequence × 1 Widom 601 sequence × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL were applied on grid and immediately blotted for 2.5 s at blot force 0. Resolution 6.60 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHD1L_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 2–865; UniProt 16–879

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 9t4v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t4v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t4v
Deposition date deposition_date2025-11-02
Structure title titleALC1/CHD1L in an intermediate conformation, bound to a PARylated nucleosome
Keywords keywordsALC1, CHD1L, chromatin remodeler, DNA damage response, nucleosome, poly(ADP-ribose), 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_guinier49.75
Radius of gyration Rg (electron density) rg_electron49.57
Forward intensity I(0) i01640190000.00
Molecular weight molecular_weight274160.0 kDa
Excluded volume excluded_volume317630 ų
Envelope volume envelope_volume513730 ų
Hydration-shell volume shell_volume87794 ų
Envelope diameter envelope_diameter173.8
Shell Rg shell_rg52.21
Envelope Rg envelope_rg48.69
Shape Rg shape_rg49.56
Total Rg total_rg49.69
Total atoms total_atoms35422
Residues n_residues1908
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 dmax174.9
Rg (real space) rg_real49.86
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real1.6400e+09
I(0) uncertainty (real space) i0_real_error3.1290e+07
Rg (reciprocal space) rg_reciprocal49.75
I(0) (reciprocal space) i0_reciprocal1640000000.0000
Solution quality estimate total_estimate0.8473
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.1
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.107
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha193500000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.737; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.805

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (2)

9. Files and Curves (10)