8bot

Cryo-EM structure of NHEJ supercomplex(trimer)

Method: ELECTRON MICROSCOPY Dmax: 338.4 Å Quality: EXCELLENT

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

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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain K; UniProt 1–336 Chain L; UniProt 1–336 Chain N; UniProt 1–336 Chain O; UniProt 1–336 Not recorded DNA ligase 4 × 2 (P49917) Non-homologous end-joining factor 1 × 4 (Q9H9Q4) DNA-dependent protein kinase catalytic subunit × 3 (P78527) X-ray repair cross-complementing protein 6 × 3 (P12956) X-ray repair cross-complementing protein 5 × 3 (P13010) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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 1
Chains and sequence ranges Author chain K; PDBConstruct 1–336; UniProt 1–336 Author chain L; PDBConstruct 1–336; UniProt 1–336 Author chain N; PDBConstruct 1–336; UniProt 1–336 Author chain O; 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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain M; UniProt 1–911 Chain P; UniProt 1–911 Not recorded DNA repair protein XRCC4 × 4 (Q13426) Non-homologous end-joining factor 1 × 4 (Q9H9Q4) DNA-dependent protein kinase catalytic subunit × 3 (P78527) X-ray repair cross-complementing protein 6 × 3 (P12956) X-ray repair cross-complementing protein 5 × 3 (P13010) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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 2
Chains and sequence ranges Author chain M; PDBConstruct 1–911; UniProt 1–911 Author chain P; PDBConstruct 1–911; UniProt 1–911

Non-homologous end-joining factor 1

Homo sapiens

UniProt Q9H9Q4

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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain Q; UniProt 1–299 Chain R; UniProt 1–299 Chain X; UniProt 1–299 Chain Y; UniProt 1–299 Not recorded DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA-dependent protein kinase catalytic subunit × 3 (P78527) X-ray repair cross-complementing protein 6 × 3 (P12956) X-ray repair cross-complementing protein 5 × 3 (P13010) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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.

25 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NHEJ1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain Q; PDBConstruct 1–299; UniProt 1–299 Author chain R; PDBConstruct 1–299; UniProt 1–299 Author chain X; PDBConstruct 1–299; UniProt 1–299 Author chain Y; PDBConstruct 1–299; UniProt 1–299

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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain A; UniProt 1–4128 Chain F; UniProt 1–4128 Chain S; UniProt 1–4128 Not recorded DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) Non-homologous end-joining factor 1 × 4 (Q9H9Q4) X-ray repair cross-complementing protein 6 × 3 (P12956) X-ray repair cross-complementing protein 5 × 3 (P13010) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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 4
Chains and sequence ranges Author chain A; PDBConstruct 1–4128; UniProt 1–4128 Author chain F; 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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain B; UniProt 1–609 Chain G; UniProt 1–609 Chain T; UniProt 1–609 Not recorded DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) Non-homologous end-joining factor 1 × 4 (Q9H9Q4) DNA-dependent protein kinase catalytic subunit × 3 (P78527) X-ray repair cross-complementing protein 5 × 3 (P13010) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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 5
Chains and sequence ranges Author chain B; PDBConstruct 1–609; UniProt 1–609 Author chain G; 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 × 19 DNA 6 PDB declaration: 25-meric(25) Consistent with all polymer counts Chain C; UniProt 1–732 Chain H; UniProt 1–732 Chain U; UniProt 1–732 Not recorded DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) Non-homologous end-joining factor 1 × 4 (Q9H9Q4) DNA-dependent protein kinase catalytic subunit × 3 (P78527) X-ray repair cross-complementing protein 6 × 3 (P12956) DNA (28-MER) × 2 DNA (27-MER) × 2 DNA (24-MER) × 1 DNA (24-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.76 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 6
Chains and sequence ranges Author chain C; PDBConstruct 1–732; UniProt 1–732 Author chain H; PDBConstruct 1–732; UniProt 1–732 Author chain U; PDBConstruct 1–732; UniProt 1–732

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 8bot

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8bot
Deposition date deposition_date2022-11-15
Structure title titleCryo-EM structure of NHEJ supercomplex(trimer)
Keywords keywordsNHEJ, DNA-PK, DNA-PKcs, Ku70, Ku80, XLF, DNA repair, 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_electron117.70
Forward intensity I(0) i045208500000.00
Molecular weight molecular_weight1840000.0 kDa
Excluded volume excluded_volume2309700 ų
Envelope volume envelope_volume4504000 ų
Hydration-shell volume shell_volume323250 ų
Envelope diameter envelope_diameter394.3
Shell Rg shell_rg115.40
Envelope Rg envelope_rg108.80
Shape Rg shape_rg117.80
Total Rg total_rg117.70
Total atoms total_atoms129197
Residues n_residues16164
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 dmax338.4
Rg (real space) rg_real118.20
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real4.3940e+10
I(0) uncertainty (real space) i0_real_error9.5280e+08
Rg (reciprocal space) rg_reciprocal118.00
I(0) (reciprocal space) i0_reciprocal45090000000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary156.2
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha2.0500
Highest regularization parameter α highest_alpha1378000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.913; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; 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)