8x7k

Cryo-EM structures of RNF168/UbcH5c-Ub in complex with H2AK13Ub nucleosomes determined by activity-based chemical trapping strategy (adjacent H2AK13/15 dual-monoubiquitination)

Method: ELECTRON MICROSCOPY Dmax: 126.9 Å Quality: EXCELLENT

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

Histone H3.2

Homo sapiens

UniProt Q71DI3

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 39–135 Chain E; UniProt 39–135 Not recorded Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H2A type 1-B/E × 1 (P04908) DNA (143-MER) × 1 DNA (143-MER) × 1 Ubiquitin-conjugating enzyme E2 D3 × 1 (P61077) 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 3.27 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.

139 other PDB entries and 157 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–97; UniProt 39–135 Author chain E; PDBConstruct 1–97; UniProt 39–135

Histone H4

Homo sapiens

UniProt P62805

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 21–102 Chain F; UniProt 21–102 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H2A type 1-B/E × 1 (P04908) DNA (143-MER) × 1 DNA (143-MER) × 1 Ubiquitin-conjugating enzyme E2 D3 × 1 (P61077) 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 3.27 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–82; UniProt 21–102 Author chain F; PDBConstruct 1–82; UniProt 21–102

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 15–119 Chain G; UniProt 11–118 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2B type 1-K × 2 (O60814) DNA (143-MER) × 1 DNA (143-MER) × 1 Ubiquitin-conjugating enzyme E2 D3 × 1 (P61077) 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 3.27 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 3, 5
Chains and sequence ranges Author chain C; PDBConstruct 1–105; UniProt 15–119 Author chain G; PDBConstruct 1–108; UniProt 11–118

Histone H2B type 1-K

Homo sapiens

UniProt O60814

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 32–125 Chain H; UniProt 32–125 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2A type 1-B/E × 1 (P04908) DNA (143-MER) × 1 DNA (143-MER) × 1 Ubiquitin-conjugating enzyme E2 D3 × 1 (P61077) 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 3.27 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.

82 other PDB entries and 82 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1K_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–94; UniProt 32–125 Author chain H; PDBConstruct 1–94; UniProt 32–125

Ubiquitin-conjugating enzyme E2 D3

Homo sapiens

UniProt P61077

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 1–147 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H2A type 1-B/E × 1 (P04908) DNA (143-MER) × 1 DNA (143-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 3.27 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.

45 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D3_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain K; PDBConstruct 1–147; UniProt 1–147

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain L; UniProt 1–113 Not recorded Histone H3.2 × 2 (Q71DI3) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 1 (P04908) Histone H2B type 1-K × 2 (O60814) Histone H2A type 1-B/E × 1 (P04908) DNA (143-MER) × 1 DNA (143-MER) × 1 Ubiquitin-conjugating enzyme E2 D3 × 1 (P61077) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 9
Chains and sequence ranges Author chain L; PDBConstruct 1–113; UniProt 1–113

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 8x7k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x7k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x7k
Deposition date deposition_date2023-11-24
Structure title titleCryo-EM structures of RNF168/UbcH5c-Ub in complex with H2AK13Ub nucleosomes determined by activity-based chemical trapping strategy (adjacent H2AK13/15 dual-monoubiquitination)
Keywords keywordsRNF168, nucleosome, H2AK13/15 ubiquitination, NUCLEAR PROTEIN, NUCLEAR PROTEIN-DNA complex; NUCLEAR PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.57
Radius of gyration Rg (electron density) rg_electron39.52
Forward intensity I(0) i0968027000.00
Molecular weight molecular_weight195680.0 kDa
Excluded volume excluded_volume220010 ų
Envelope volume envelope_volume328380 ų
Hydration-shell volume shell_volume68077 ų
Envelope diameter envelope_diameter136.8
Shell Rg shell_rg46.36
Envelope Rg envelope_rg38.73
Shape Rg shape_rg39.41
Total Rg total_rg40.08
Total atoms total_atoms13387
Residues n_residues1240
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 dmax126.9
Rg (real space) rg_real41.34
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real9.6800e+08
I(0) uncertainty (real space) i0_real_error1.7980e+07
Rg (reciprocal space) rg_reciprocal41.57
I(0) (reciprocal space) i0_reciprocal968300000.0000
Solution quality estimate total_estimate0.9029
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.1
Skewness Skewness skewness0.050
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58450000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)