8bh3

DNA-PK Ku80 mediated dimer bound to PAXX

Method: ELECTRON MICROSCOPY Dmax: 300.2 Å Quality: EXCELLENT

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

DNA-dependent protein kinase catalytic subunit

OrganismNot specified

UniProt P78527

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain A; UniProt 1–4128 Chain S; UniProt 1–4128 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Protein PAXX × 2 (Q9BUH6) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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.

46 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRKDC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–4128; UniProt 1–4128 Author chain S; PDBConstruct 1–4128; UniProt 1–4128

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain B; UniProt 1–609 Chain T; UniProt 1–609 Not recorded DNA-dependent protein kinase catalytic subunit × 2 (P78527) X-ray repair cross-complementing protein 5 × 2 (P13010) Protein PAXX × 2 (Q9BUH6) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–609; UniProt 1–609 Author chain T; 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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain C; UniProt 1–732 Chain L; UniProt 1–732 Not recorded DNA-dependent protein kinase catalytic subunit × 2 (P78527) X-ray repair cross-complementing protein 6 × 2 (P12956) Protein PAXX × 2 (Q9BUH6) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–732; UniProt 1–732 Author chain L; PDBConstruct 1–732; UniProt 1–732

Protein PAXX

Homo sapiens

UniProt Q9BUH6

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain D; UniProt 1–204 Chain M; UniProt 1–204 Not recorded DNA-dependent protein kinase catalytic subunit × 2 (P78527) X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAXX_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–204; UniProt 1–204 Author chain M; PDBConstruct 1–204; UniProt 1–204

DNA repair protein XRCC4

Homo sapiens

UniProt Q13426

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain G; UniProt 1–336 Chain H; UniProt 1–336 Chain P; UniProt 1–336 Chain Q; UniProt 1–336 Not recorded DNA-dependent protein kinase catalytic subunit × 2 (P78527) X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Protein PAXX × 2 (Q9BUH6) DNA ligase 4 × 2 (P49917) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XRCC4_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–336; UniProt 1–336 Author chain H; PDBConstruct 1–336; UniProt 1–336 Author chain P; PDBConstruct 1–336; UniProt 1–336 Author chain Q; PDBConstruct 1–336; UniProt 1–336

DNA ligase 4

Homo sapiens

UniProt P49917

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain I; UniProt 1–911 Chain R; UniProt 1–911 Not recorded DNA-dependent protein kinase catalytic subunit × 2 (P78527) X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Protein PAXX × 2 (Q9BUH6) DNA repair protein XRCC4 × 4 (Q13426) DNA (25-MER) × 1 DNA (27-MER) × 1 DNA (26-MER) × 1 DNA (28-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.55 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.

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

View Construct and Data Evidence
UniProt name DNLI4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–911; UniProt 1–911 Author chain R; PDBConstruct 1–911; UniProt 1–911

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 8bh3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bh3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bh3
Deposition date deposition_date2022-10-28
Structure title titleDNA-PK Ku80 mediated dimer bound to PAXX
Keywords keywordsDNA-PK, DNA-PKcs, Ku70, Ku80, PAXX, NHEJ, 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_guinier
Radius of gyration Rg (electron density) rg_electron115.60
Forward intensity I(0) i021679500000.00
Molecular weight molecular_weight1270900.0 kDa
Excluded volume excluded_volume1595100 ų
Envelope volume envelope_volume3153900 ų
Hydration-shell volume shell_volume235210 ų
Envelope diameter envelope_diameter397.5
Shell Rg shell_rg100.20
Envelope Rg envelope_rg110.50
Shape Rg shape_rg115.70
Total Rg total_rg115.40
Total atoms total_atoms89245
Residues n_residues11118
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 dmax300.2
Rg (real space) rg_real110.00
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real2.0690e+10
I(0) uncertainty (real space) i0_real_error3.8520e+08
Rg (reciprocal space) rg_reciprocal108.00
I(0) (reciprocal space) i0_reciprocal21100000000.0000
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_primary92.4
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.929
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha1.1130
Highest regularization parameter α highest_alpha659900000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 1.000; Stabil: 0.968; Sysdev: 1.000; Positv: 1.000; Valcen: 0.842; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)