6i8a

The crystal structure of the Pol2 catalytic domain of DNA polymerase epsilon carrying a P301R substitution.

Method: X-RAY DIFFRACTION Dmax: 176.4 Å Quality: GOOD

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

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P21951

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 A; UniProt 1–1185 Mutation:P301R Primer DNA × 1 Template DNA × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 FE FE (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;292 K;50mM MES pH 6.5, 150mM NaAc, 8%PEG20K Resolution 2.65 Å R-free 0.279
2 Protein–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain B; UniProt 1–1185 Mutation:P301R Primer DNA × 1 Template DNA × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 2 FE FE (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;292 K;50mM MES pH 6.5, 150mM NaAc, 8%PEG20K Resolution 2.65 Å R-free 0.279

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.

33 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–1190; UniProt 1–1185 Author chain B; PDBConstruct 6–1190; UniProt 1–1185

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 6i8a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6i8a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6i8a
Deposition date deposition_date2018-11-19
Structure title titleThe crystal structure of the Pol2 catalytic domain of DNA polymerase epsilon carrying a P301R substitution.
Keywords keywordsDNA, Pol2, P301R, P286R, cancer, endometrial, DNA binding protein, Pol epsilon; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier51.19
Radius of gyration Rg (electron density) rg_electron51.92
Forward intensity I(0) i01018560000.00
Molecular weight molecular_weight257050.0 kDa
Excluded volume excluded_volume317340 ų
Envelope volume envelope_volume470780 ų
Hydration-shell volume shell_volume77059 ų
Envelope diameter envelope_diameter180.7
Shell Rg shell_rg52.94
Envelope Rg envelope_rg50.99
Shape Rg shape_rg51.97
Total Rg total_rg51.78
Total atoms total_atoms18059
Residues n_residues2251
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 dmax176.4
Rg (real space) rg_real51.42
Rg uncertainty (real space) rg_real_error2.02
I(0) (real space) i0_real1.0190e+09
I(0) uncertainty (real space) i0_real_error2.1200e+07
Rg (reciprocal space) rg_reciprocal50.99
I(0) (reciprocal space) i0_reciprocal1018000000.0000
Solution quality estimate total_estimate0.8328
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis-0.528
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.859; Smooth: 0.772

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)