9b8r

Cryo-EM structure of S. cerevisiae PolE-core-DNA

Method: ELECTRON MICROSCOPY Dmax: 101.3 Å Quality: EXCELLENT

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

DNA polymerase epsilon catalytic subunit

Saccharomyces cerevisiae

UniProt A0A8H4BWE7

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 Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain E; UniProt 27–1186 Not recorded Primer DNA × 1 Template DNA × 1 SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4BWE7_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–1160; UniProt 27–1186

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 9b8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b8r
Deposition date deposition_date2024-03-31
Structure title titleCryo-EM structure of S. cerevisiae PolE-core-DNA
Keywords keywordsPol2, DNA, REPLICATION, 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_guinier33.77
Radius of gyration Rg (electron density) rg_electron33.10
Forward intensity I(0) i0295847000.00
Molecular weight molecular_weight134360.0 kDa
Excluded volume excluded_volume166440 ų
Envelope volume envelope_volume225540 ų
Hydration-shell volume shell_volume54595 ų
Envelope diameter envelope_diameter106.3
Shell Rg shell_rg41.75
Envelope Rg envelope_rg32.62
Shape Rg shape_rg33.11
Total Rg total_rg33.75
Total atoms total_atoms9425
Residues n_residues1141
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 dmax101.3
Rg (real space) rg_real33.56
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real2.9580e+08
I(0) uncertainty (real space) i0_real_error4.3520e+06
Rg (reciprocal space) rg_reciprocal33.69
I(0) (reciprocal space) i0_reciprocal295900000.0000
Solution quality estimate total_estimate0.9055
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.3
Skewness Skewness skewness0.058
Kurtosis Kurtosis kurtosis-0.553
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50520000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.959

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)