9iax

DNA-PK, LX4, XLF - Catalytic domain of L4

Method: ELECTRON MICROSCOPY Dmax: 277.1 Å Quality: GOOD

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–4128 Not recorded X-ray repair cross-complementing protein 6 × 1 (P12956) X-ray repair cross-complementing protein 5 × 1 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 2 (Q13426) DNA ligase 4 × 1 (P49917) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 1–609 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) X-ray repair cross-complementing protein 5 × 1 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 2 (Q13426) DNA ligase 4 × 1 (P49917) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–732 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) X-ray repair cross-complementing protein 6 × 1 (P12956) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 2 (Q13426) DNA ligase 4 × 1 (P49917) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 1–299 Chain M; UniProt 1–299 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) X-ray repair cross-complementing protein 6 × 1 (P12956) X-ray repair cross-complementing protein 5 × 1 (P13010) DNA repair protein XRCC4 × 2 (Q13426) DNA ligase 4 × 1 (P49917) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–299; UniProt 1–299 Author chain M; PDBConstruct 1–299; UniProt 1–299

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain G; UniProt 1–336 Chain H; UniProt 1–336 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) X-ray repair cross-complementing protein 6 × 1 (P12956) X-ray repair cross-complementing protein 5 × 1 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA ligase 4 × 1 (P49917) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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

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 × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain K; UniProt 1–911 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) X-ray repair cross-complementing protein 6 × 1 (P12956) X-ray repair cross-complementing protein 5 × 1 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 2 (Q13426) DNA × 1 DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.97 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 K; 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 9iax

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9iax
Deposition date deposition_date2025-02-11
Structure title titleDNA-PK, LX4, XLF - Catalytic domain of L4
Keywords keywordsKinase, NHEJ, cryo-EM, DNA-PK, 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_guinier74.12
Radius of gyration Rg (electron density) rg_electron74.38
Forward intensity I(0) i07244250000.00
Molecular weight molecular_weight729790.0 kDa
Excluded volume excluded_volume916910 ų
Envelope volume envelope_volume1553900 ų
Hydration-shell volume shell_volume175180 ų
Envelope diameter envelope_diameter269.3
Shell Rg shell_rg72.27
Envelope Rg envelope_rg74.40
Shape Rg shape_rg74.43
Total Rg total_rg74.17
Total atoms total_atoms51268
Residues n_residues6382
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 dmax277.1
Rg (real space) rg_real78.52
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real7.3080e+09
I(0) uncertainty (real space) i0_real_error1.6030e+08
Rg (reciprocal space) rg_reciprocal73.68
I(0) (reciprocal space) i0_reciprocal7236000000.0000
Solution quality estimate total_estimate0.8619
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.4
Skewness Skewness skewness0.628
Kurtosis Kurtosis kurtosis0.163
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.9431
Highest regularization parameter α highest_alpha547400000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.706; Stabil: 0.847; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.590

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)