8g6s

H2AK119ub-modified nucleosome ubiquitin position 2

Method: ELECTRON MICROSCOPY Dmax: 130.5 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 1–136 Chain E; UniProt 1–136 Mutation:G102A Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 601 DNA (147-MER) × 1 601 DNA (147-MER) × 1 Ubiquitin × 1 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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

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 × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 601 DNA (147-MER) × 1 601 DNA (147-MER) × 1 Ubiquitin × 1 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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

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: 11-meric(11) Consistent with all polymer counts Chain C; UniProt 1–130 Chain G; UniProt 1–130 Mutation:K119C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2B 1.1 × 2 (P02281) 601 DNA (147-MER) × 1 601 DNA (147-MER) × 1 Ubiquitin × 1 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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 1–130; 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 Mutation:S33T Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) 601 DNA (147-MER) × 1 601 DNA (147-MER) × 1 Ubiquitin × 1 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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

Ubiquitin

Homo sapiens

UniProt P0CG47

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 1–76 Mutation:G76C Histone H3.2 × 2 (P84233) Histone H4 × 2 (P62799) Histone H2A × 2 (Q6AZJ8) Histone H2B 1.1 × 2 (P02281) 601 DNA (147-MER) × 1 601 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 5–80; UniProt 1–76

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 8g6s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g6s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g6s
Deposition date deposition_date2023-02-15
Structure title titleH2AK119ub-modified nucleosome ubiquitin position 2
Keywords keywordsnucleosome, ubiquitin, histone, chromatin, 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_guinier42.50
Radius of gyration Rg (electron density) rg_electron40.29
Forward intensity I(0) i0873773000.00
Molecular weight molecular_weight182680.0 kDa
Excluded volume excluded_volume203790 ų
Envelope volume envelope_volume326170 ų
Hydration-shell volume shell_volume66889 ų
Envelope diameter envelope_diameter137.7
Shell Rg shell_rg46.71
Envelope Rg envelope_rg39.35
Shape Rg shape_rg40.16
Total Rg total_rg40.87
Total atoms total_atoms12480
Residues n_residues1114
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 dmax130.5
Rg (real space) rg_real42.30
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real8.7380e+08
I(0) uncertainty (real space) i0_real_error1.3300e+07
Rg (reciprocal space) rg_reciprocal42.49
I(0) (reciprocal space) i0_reciprocal874000000.0000
Solution quality estimate total_estimate0.8992
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.113
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72730000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)