9kq2

Cryo-EM structure of RNF168'-RNF168-UbcH5c complex bound to nucleosome

Method: ELECTRON MICROSCOPY Dmax: 117.2 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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 2–136 Chain E; UniProt 2–136 Not recorded Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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 1–135; UniProt 2–136 Author chain E; PDBConstruct 1–135; UniProt 2–136

Histone H4

Xenopus laevis

UniProt A0A8J1LTD2

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 15–116 Chain F; UniProt 15–116 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8J1LTD2_XENLA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–102; UniProt 15–116 Author chain F; PDBConstruct 1–102; UniProt 15–116

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 2–130 Chain G; UniProt 2–130 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–129; UniProt 2–130 Author chain G; PDBConstruct 1–129; UniProt 2–130

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 5–126 Chain H; UniProt 5–126 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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 1–122; UniProt 5–126 Author chain H; PDBConstruct 1–122; UniProt 5–126

E3 ubiquitin-protein ligase RNF168

Homo sapiens

UniProt Q8IYW5

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 1–103 Not recorded Histone H3 × 2 (A0A310TTQ1) Histone H4 × 2 (A0A8J1LTD2) Histone H2A × 2 (Q6AZJ8) Histone H2B × 2 (A0A8J0U496) DNA (147-MER) × 1 DNA (147-MER) × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

38 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RN168_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain K; PDBConstruct 1–103; UniProt 1–103

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 9kq2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kq2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9kq2
Deposition date deposition_date2024-11-25
最后修订 last_revision2025-11-12
Structure title titleCryo-EM structure of RNF168'-RNF168-UbcH5c complex bound to nucleosome
Keywords keywords;DNA repair, Histone ubiquitination, Nucleosome, E3 ubiquitin-protein ligase, RNF168, 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_guinier41.13
Radius of gyration Rg (electron density) rg_electron38.54
Forward intensity I(0) i0888228000.00
Molecular weight molecular_weight183400.0 kDa
Excluded volume excluded_volume204260 ų
Envelope volume envelope_volume317770 ų
Hydration-shell volume shell_volume67024 ų
Envelope diameter envelope_diameter118.6
Shell Rg shell_rg46.08
Envelope Rg envelope_rg37.68
Shape Rg shape_rg38.37
Total Rg total_rg39.25
Total atoms total_atoms12514
Residues n_residues1118
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 dmax117.2
Rg (real space) rg_real40.90
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real8.8820e+08
I(0) uncertainty (real space) i0_real_error1.4060e+07
Rg (reciprocal space) rg_reciprocal41.13
I(0) (reciprocal space) i0_reciprocal888400000.0000
Solution quality estimate total_estimate0.8439
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.029
Kurtosis Kurtosis kurtosis-0.686
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53760000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.990; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)