8txv

Cryo-EM structure of the human nucleosome core particle ubiquitylated at histone H2A K15 in complex with RNF168 (Class 1)

Method: ELECTRON MICROSCOPY Dmax: 135.5 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

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 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) Polyubiquitin-B × 1 (P0CG47) Histone H2A type 1-B/E × 2 (P04908) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–140; UniProt 1–136 Author chain E; PDBConstruct 5–140; UniProt 1–136

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 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.1 × 2 (P68431) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) Polyubiquitin-B × 1 (P0CG47) Histone H2A type 1-B/E × 2 (P04908) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 5–107; UniProt 1–103 Author chain F; PDBConstruct 5–107; UniProt 1–103

Histone H2B type 1-C/E/F/G/I

Homo sapiens

UniProt P62807

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 1–124 Chain H; UniProt 1–124 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) Polyubiquitin-B × 1 (P0CG47) Histone H2A type 1-B/E × 2 (P04908) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

79 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1C_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 5–128; UniProt 1–124 Author chain H; PDBConstruct 5–128; UniProt 1–124

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 K; UniProt 1–571 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (147-MER) × 1 DNA (147-MER) × 1 Polyubiquitin-B × 1 (P0CG47) Histone H2A type 1-B/E × 2 (P04908) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 6
Chains and sequence ranges Author chain K; PDBConstruct 4–574; UniProt 1–571

Polyubiquitin-B

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 × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain M; UniProt 18–76 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) Histone H2A type 1-B/E × 2 (P04908) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 M; PDBConstruct 23–81; UniProt 18–76

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 12–130 Chain G; UniProt 12–130 Mutation:K13S Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-C/E/F/G/I × 2 (P62807) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) Polyubiquitin-B × 1 (P0CG47) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 8
Chains and sequence ranges Author chain C; PDBConstruct 1–119; UniProt 12–130 Author chain G; PDBConstruct 1–119; UniProt 12–130

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 8txv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8txv
Deposition date deposition_date2023-08-24
Structure title titleCryo-EM structure of the human nucleosome core particle ubiquitylated at histone H2A K15 in complex with RNF168 (Class 1)
Keywords keywords;Nucleosome core particle, chromatin, RNF168, MIU2-LRM domains, DNA repair, DNA double-strand break, Homologous recombination, BRCA1-BARD1, 53BP1, ubiquitin, STRUCTURAL PROTEIN-DNA-TRANSFERASE complex, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.70
Radius of gyration Rg (electron density) rg_electron39.49
Forward intensity I(0) i0922095000.00
Molecular weight molecular_weight187720.0 kDa
Excluded volume excluded_volume209490 ų
Envelope volume envelope_volume324450 ų
Hydration-shell volume shell_volume67489 ų
Envelope diameter envelope_diameter143.8
Shell Rg shell_rg46.22
Envelope Rg envelope_rg38.80
Shape Rg shape_rg39.35
Total Rg total_rg40.10
Total atoms total_atoms12824
Residues n_residues1151
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 dmax135.5
Rg (real space) rg_real41.52
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real9.2210e+08
I(0) uncertainty (real space) i0_real_error1.7580e+07
Rg (reciprocal space) rg_reciprocal41.70
I(0) (reciprocal space) i0_reciprocal922300000.0000
Solution quality estimate total_estimate0.8920
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.9
Skewness Skewness skewness0.114
Kurtosis Kurtosis kurtosis-0.592
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha82090000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)