7tyr

Cryo-EM structure of the basal state of the Artemis:DNA-PKcs complex (see COMPND 13/14)

Method: ELECTRON MICROSCOPY Dmax: 182.1 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–4128 Not recorded Protein artemis × 1 (Q96SD1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge-freeze was performed using a home-made manual plunger at typical indoor humidity (Los Angeles, CA) and at room temperature. Resolution 3.33 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

Protein artemis

Homo sapiens

UniProt Q96SD1

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–692 Not recorded DNA-dependent protein kinase catalytic subunit × 1 (P78527) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Plunge-freeze was performed using a home-made manual plunger at typical indoor humidity (Los Angeles, CA) and at room temperature. Resolution 3.33 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCR1C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–692; UniProt 1–692

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 7tyr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tyr
Deposition date deposition_date2022-02-14
Structure title titleCryo-EM structure of the basal state of the Artemis:DNA-PKcs complex (see COMPND 13/14)
Keywords keywordsKinase, nuclease, 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_guinier56.67
Radius of gyration Rg (electron density) rg_electron56.18
Forward intensity I(0) i02732490000.00
Molecular weight molecular_weight449690.0 kDa
Excluded volume excluded_volume567340 ų
Envelope volume envelope_volume888480 ų
Hydration-shell volume shell_volume127850 ų
Envelope diameter envelope_diameter183.5
Shell Rg shell_rg62.63
Envelope Rg envelope_rg54.17
Shape Rg shape_rg56.18
Total Rg total_rg56.34
Total atoms total_atoms31599
Residues n_residues3957
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 dmax182.1
Rg (real space) rg_real56.43
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real2.7320e+09
I(0) uncertainty (real space) i0_real_error5.1080e+07
Rg (reciprocal space) rg_reciprocal56.85
I(0) (reciprocal space) i0_reciprocal2734000000.0000
Solution quality estimate total_estimate0.6624
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.5
Skewness Skewness skewness0.151
Kurtosis Kurtosis kurtosis-0.511
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.973; Smooth: 0.797

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)