8rd4

Telomeric RAP1:DNA-PK complex

Method: ELECTRON MICROSCOPY Dmax: 253.4 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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–4128 Not recorded Telomeric repeat-binding factor 2-interacting protein 1 × 1 (Q9NYB0) X-ray repair cross-complementing protein 6 × 1 (P12956) X-ray repair cross-complementing protein 5 × 1 (P13010) DNA (41-MER) × 1 DNA (41-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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

Telomeric repeat-binding factor 2-interacting protein 1

Homo sapiens

UniProt Q9NYB0

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 1–399 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 (41-MER) × 1 DNA (41-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TE2IP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–399; UniProt 1–399

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain E; UniProt 1–609 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) Telomeric repeat-binding factor 2-interacting protein 1 × 1 (Q9NYB0) X-ray repair cross-complementing protein 5 × 1 (P13010) DNA (41-MER) × 1 DNA (41-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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 3
Chains and sequence ranges Author chain E; 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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain F; UniProt 1–732 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) Telomeric repeat-binding factor 2-interacting protein 1 × 1 (Q9NYB0) X-ray repair cross-complementing protein 6 × 1 (P12956) DNA (41-MER) × 1 DNA (41-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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 4
Chains and sequence ranges Author chain F; 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 8rd4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rd4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rd4
Deposition date deposition_date2023-12-07
Structure title titleTelomeric RAP1:DNA-PK complex
Keywords keywordsTelomere NHEJ BRCT domain SAP domain, 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_guinier66.62
Radius of gyration Rg (electron density) rg_electron66.27
Forward intensity I(0) i04722530000.00
Molecular weight molecular_weight580660.0 kDa
Excluded volume excluded_volume726810 ų
Envelope volume envelope_volume1138200 ų
Hydration-shell volume shell_volume142480 ų
Envelope diameter envelope_diameter230.9
Shell Rg shell_rg68.06
Envelope Rg envelope_rg64.12
Shape Rg shape_rg66.27
Total Rg total_rg66.29
Total atoms total_atoms40711
Residues n_residues4950
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 dmax253.4
Rg (real space) rg_real71.03
Rg uncertainty (real space) rg_real_error1.59
I(0) (real space) i0_real4.7730e+09
I(0) uncertainty (real space) i0_real_error8.0790e+07
Rg (reciprocal space) rg_reciprocal66.56
I(0) (reciprocal space) i0_reciprocal4722000000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.9
Skewness Skewness skewness0.599
Kurtosis Kurtosis kurtosis0.188
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.9250
Highest regularization parameter α highest_alpha432800000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.752; Stabil: 0.830; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.794

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)