9n82

The ligation (AMP-Lys) complex in the NHEJ pathway

Method: ELECTRON MICROSCOPY Dmax: 285.1 Å Quality: EXCELLENT

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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain A; UniProt 1–609 Chain a; UniProt 1–609 Not recorded X-ray repair cross-complementing protein 5 × 2 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) Protein PAXX × 2 (Q9BUH6) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 A; PDBConstruct 4–612; UniProt 1–609 Author chain a; PDBConstruct 4–612; 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 B; UniProt 1–732 Chain b; UniProt 1–732 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) Protein PAXX × 2 (Q9BUH6) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 B; PDBConstruct 1–732; UniProt 1–732 Author chain b; 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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain C; UniProt 1–299 Chain c; UniProt 1–299 Not recorded 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) Protein PAXX × 2 (Q9BUH6) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 C; PDBConstruct 4–302; UniProt 1–299 Author chain c; PDBConstruct 4–302; 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 × 14 DNA 4 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain D; UniProt 1–336 Chain E; UniProt 1–336 Chain d; UniProt 1–336 Chain e; UniProt 1–336 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA ligase 4 × 2 (P49917) Protein PAXX × 2 (Q9BUH6) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–336; UniProt 1–336 Author chain E; PDBConstruct 1–336; UniProt 1–336 Author chain d; PDBConstruct 1–336; UniProt 1–336 Author chain e; 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 F; UniProt 1–911 Chain f; UniProt 1–911 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 4 (Q13426) Protein PAXX × 2 (Q9BUH6) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 5
Chains and sequence ranges Author chain F; PDBConstruct 4–914; UniProt 1–911 Author chain f; PDBConstruct 4–914; UniProt 1–911

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 G; UniProt 1–204 Chain H; UniProt 1–204 Not recorded X-ray repair cross-complementing protein 6 × 2 (P12956) X-ray repair cross-complementing protein 5 × 2 (P13010) Non-homologous end-joining factor 1 × 2 (Q9H9Q4) DNA repair protein XRCC4 × 4 (Q13426) DNA ligase 4 × 2 (P49917) DNA (39-MER) × 1 DNA (38-MER) × 1 DNA (35-MER) × 1 DNA (34-MER) × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 6
Chains and sequence ranges Author chain G; PDBConstruct 15–218; UniProt 1–204 Author chain H; PDBConstruct 15–218; UniProt 1–204

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 9n82

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n82
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n82
Deposition date deposition_date2025-02-07
Structure title titleThe ligation (AMP-Lys) complex in the NHEJ pathway
Keywords keywordsNHEJ, ligation, XLF, PAXX, DNA repair, Ligase IV, LIGASE-TRANSFERASE-DNA complex; LIGASE/TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.18
Radius of gyration Rg (electron density) rg_electron79.51
Forward intensity I(0) i04406090000.00
Molecular weight molecular_weight540170.0 kDa
Excluded volume excluded_volume666850 ų
Envelope volume envelope_volume1220400 ų
Hydration-shell volume shell_volume131790 ų
Envelope diameter envelope_diameter261.1
Shell Rg shell_rg71.47
Envelope Rg envelope_rg76.72
Shape Rg shape_rg79.54
Total Rg total_rg79.28
Total atoms total_atoms37801
Residues n_residues4470
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 dmax285.1
Rg (real space) rg_real83.61
Rg uncertainty (real space) rg_real_error1.97
I(0) (real space) i0_real4.4380e+09
I(0) uncertainty (real space) i0_real_error8.7260e+07
Rg (reciprocal space) rg_reciprocal79.02
I(0) (reciprocal space) i0_reciprocal4404000000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.8
Skewness Skewness skewness0.417
Kurtosis Kurtosis kurtosis-0.172
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha1.0700
Highest regularization parameter α highest_alpha161900000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 0.836; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.569

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)