9l43

ATR Spiral -ATRIP bound with VE-822

Method: ELECTRON MICROSCOPY Dmax: 173.5 Å Quality: GOOD

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

Serine/threonine-protein kinase ATR

Homo sapiens

UniProt Q13535

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–2644 Chain B; UniProt 1–2644 Not recorded ATR-interacting protein × 2 (Q8WXE1) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.83 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2644; UniProt 1–2644 Author chain B; PDBConstruct 1–2644; UniProt 1–2644

ATR-interacting protein

Homo sapiens

UniProt Q8WXE1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–791 Chain D; UniProt 1–791 Not recorded Serine/threonine-protein kinase ATR × 2 (Q13535) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.83 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATRIP_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–791; UniProt 1–791 Author chain D; PDBConstruct 1–791; UniProt 1–791

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 9l43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9l43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9l43
Deposition date deposition_date2024-12-19
Structure title titleATR Spiral -ATRIP bound with VE-822
Keywords keywordsATR spiral, ATRIP, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.42
Radius of gyration Rg (electron density) rg_electron50.05
Forward intensity I(0) i0851988000.00
Molecular weight molecular_weight245540.0 kDa
Excluded volume excluded_volume308470 ų
Envelope volume envelope_volume460590 ų
Hydration-shell volume shell_volume77813 ų
Envelope diameter envelope_diameter178.3
Shell Rg shell_rg51.80
Envelope Rg envelope_rg49.78
Shape Rg shape_rg50.07
Total Rg total_rg50.05
Total atoms total_atoms33261
Residues n_residues2415
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 dmax173.5
Rg (real space) rg_real50.54
Rg uncertainty (real space) rg_real_error1.91
I(0) (real space) i0_real8.5200e+08
I(0) uncertainty (real space) i0_real_error1.7720e+07
Rg (reciprocal space) rg_reciprocal50.32
I(0) (reciprocal space) i0_reciprocal851700000.0000
Solution quality estimate total_estimate0.8498
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.6
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.282
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61620000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.700

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)