8smy

Cryo-EM structure of the human nucleosome core particle in complex with RNF168 and UbcH5c~Ub (UbcH5c chemically conjugated to histone H2A. No density for Ub.) (class 3)

Method: ELECTRON MICROSCOPY Dmax: 130.8 Å Quality: EXCELLENT

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 H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) 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 3.20 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 H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) 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 3.20 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 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:R11S, K15C Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2B type 1-J × 2 (P06899) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) 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 3.20 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
Chains and sequence ranges Author chain C; PDBConstruct 1–119; UniProt 12–130 Author chain G; PDBConstruct 1–119; UniProt 12–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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) Histone H2A type 1-B/E × 2 (P04908) DNA (147-MER) × 1 DNA (147-MER) × 1 E3 ubiquitin-protein ligase RNF168 × 1 (Q8IYW5) 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 3.20 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 4
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 1–93 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) DNA (147-MER) × 1 DNA (147-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 3.20 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 11–103; UniProt 1–93

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 L; UniProt 1–147 Mutation:C21I, C107A, C111D, L119K Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone H2A type 1-B/E × 2 (P04908) Histone H2B type 1-J × 2 (P06899) 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 3.20 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 L; PDBConstruct 5–151; UniProt 1–147

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 8smy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8smy
Deposition date deposition_date2023-04-26
Structure title titleCryo-EM structure of the human nucleosome core particle in complex with RNF168 and UbcH5c~Ub (UbcH5c chemically conjugated to histone H2A. No density for Ub.) (class 3)
Keywords keywords;Nucleosome core particle, chromatin, RNF168, RING domain, UbcH5c, DNA repair, DNA double-strand break, Homologous recombination, 53BP1, ubiquitin, STRUCTURAL PROTEIN-DNA-TRANSFERASE complex ;; STRUCTURAL PROTEIN/DNA/TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.26
Radius of gyration Rg (electron density) rg_electron40.17
Forward intensity I(0) i01046500000.00
Molecular weight molecular_weight204390.0 kDa
Excluded volume excluded_volume230250 ų
Envelope volume envelope_volume356480 ų
Hydration-shell volume shell_volume71885 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg47.47
Envelope Rg envelope_rg39.53
Shape Rg shape_rg40.05
Total Rg total_rg40.74
Total atoms total_atoms13982
Residues n_residues1294
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 dmax130.8
Rg (real space) rg_real42.01
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.0470e+09
I(0) uncertainty (real space) i0_real_error1.7780e+07
Rg (reciprocal space) rg_reciprocal42.25
I(0) (reciprocal space) i0_reciprocal1047000000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.060
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84510000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)