7su3

CryoEM structure of DNA-PK complex VII

Method: ELECTRON MICROSCOPY Dmax: 227.2 Å Quality: GOOD

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

DNA-dependent protein kinase catalytic subunit

Homo sapiens

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 × 3 DNA 4 PDB declaration: heptameric(7) 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) ;DNA (5'-D(*GP*CP*AP*TP*GP*CP*TP*CP*TP*AP*CP*TP*GP*CP*TP*TP*CP*GP*AP*TP*AP*TP*CP*G)-3') ; × 2 ;DNA (5'-D(*AP*AP*GP*CP*AP*GP*TP*AP*GP*AP*G)-3') ; × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 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.

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 × 3 DNA 4 PDB declaration: heptameric(7) 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) ;DNA (5'-D(*GP*CP*AP*TP*GP*CP*TP*CP*TP*AP*CP*TP*GP*CP*TP*TP*CP*GP*AP*TP*AP*TP*CP*G)-3') ; × 2 ;DNA (5'-D(*AP*AP*GP*CP*AP*GP*TP*AP*GP*AP*G)-3') ; × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 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 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 × 3 DNA 4 PDB declaration: heptameric(7) 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) ;DNA (5'-D(*GP*CP*AP*TP*GP*CP*TP*CP*TP*AP*CP*TP*GP*CP*TP*TP*CP*GP*AP*TP*AP*TP*CP*G)-3') ; × 2 ;DNA (5'-D(*AP*AP*GP*CP*AP*GP*TP*AP*GP*AP*G)-3') ; × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 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 3
Chains and sequence ranges Author chain C; 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 7su3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7su3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7su3
Deposition date deposition_date2021-11-16
Structure title titleCryoEM structure of DNA-PK complex VII
Keywords keywordsNHEJ, DNA-PK, Kinase, DNA repair, DNA BINDING PROTEIN, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.63
Radius of gyration Rg (electron density) rg_electron64.37
Forward intensity I(0) i04812170000.00
Molecular weight molecular_weight587180.0 kDa
Excluded volume excluded_volume735530 ų
Envelope volume envelope_volume1098300 ų
Hydration-shell volume shell_volume141030 ų
Envelope diameter envelope_diameter229.3
Shell Rg shell_rg65.93
Envelope Rg envelope_rg63.32
Shape Rg shape_rg64.37
Total Rg total_rg64.39
Total atoms total_atoms41176
Residues n_residues5037
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 dmax227.2
Rg (real space) rg_real64.66
Rg uncertainty (real space) rg_real_error2.60
I(0) (real space) i0_real4.8120e+09
I(0) uncertainty (real space) i0_real_error1.0860e+08
Rg (reciprocal space) rg_reciprocal64.56
I(0) (reciprocal space) i0_reciprocal4811000000.0000
Solution quality estimate total_estimate0.8646
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha469100000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7su3A01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7su3C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily410 — von Willebrand factor, type A domain
Domain ID domain_id7su3C02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1600 — Ku70; Chain: A; domain 4
Homologous superfamily homologous superfamily10
Domain ID domain_id7su3C03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily240 — Ku, C-terminal domain

8. Citations (1)

9. Files and Curves (10)