9q8x

Ku70/80 bound to a 153 bp H2AX nucleosome

Method: ELECTRON MICROSCOPY Dmax: 229.3 Å Quality: GOOD

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

X-ray repair cross-complementing protein 6

Homo sapiens

UniProt P12956

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain K; UniProt 1–609 Chain M; UniProt 1–609 Not recorded X-ray repair cross-complementing protein 5 × 2 (P13010) Histone H2AX × 2 (P16104) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

57 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XRCC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–609; UniProt 1–609 Author chain M; PDBConstruct 1–609; UniProt 1–609

X-ray repair cross-complementing protein 5

Homo sapiens

UniProt P13010

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain L; UniProt 1–732 Chain N; UniProt 1–732 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) Histone H2AX × 2 (P16104) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

62 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XRCC5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–732; UniProt 1–732 Author chain N; PDBConstruct 1–732; UniProt 1–732

Histone H2AX

Homo sapiens

UniProt P16104

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 1–143 Chain G; UniProt 1–143 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

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

View Construct and Data Evidence
UniProt name H2AX_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–143; UniProt 1–143 Author chain G; PDBConstruct 1–143; UniProt 1–143

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 1–126 Chain H; UniProt 1–126 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Histone H2AX × 2 (P16104) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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 1–126; UniProt 1–126 Author chain H; PDBConstruct 1–126; UniProt 1–126

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–136 Chain E; UniProt 1–136 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Histone H2AX × 2 (P16104) Histone H2B type 1-J × 2 (P06899) Histone H4 × 2 (P62805) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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 5
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; 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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–103 Chain F; UniProt 1–103 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Histone H2AX × 2 (P16104) Histone H2B type 1-J × 2 (P06899) Histone H3.1 × 2 (P68431) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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 6
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain F; 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 9q8x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q8x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q8x
Deposition date deposition_date2025-02-25
Structure title titleKu70/80 bound to a 153 bp H2AX nucleosome
Keywords keywordsDNA-binding protein, NHEJ, Ku70/80, nucleosome, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.35
Radius of gyration Rg (electron density) rg_electron64.55
Forward intensity I(0) i02913300000.00
Molecular weight molecular_weight395840.0 kDa
Excluded volume excluded_volume471360 ų
Envelope volume envelope_volume783560 ų
Hydration-shell volume shell_volume105720 ų
Envelope diameter envelope_diameter217.9
Shell Rg shell_rg60.63
Envelope Rg envelope_rg62.31
Shape Rg shape_rg64.64
Total Rg total_rg64.20
Total atoms total_atoms27507
Residues n_residues3097
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 dmax229.3
Rg (real space) rg_real62.71
Rg uncertainty (real space) rg_real_error2.58
I(0) (real space) i0_real2.9140e+09
I(0) uncertainty (real space) i0_real_error6.9210e+07
Rg (reciprocal space) rg_reciprocal62.07
I(0) (reciprocal space) i0_reciprocal2910000000.0000
Solution quality estimate total_estimate0.8488
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0074
Highest regularization parameter α highest_alpha184700000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.751; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.794

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)