6hv8

Cryo-EM structure of S. cerevisiae Polymerase epsilon deltacat mutant

Method: ELECTRON MICROSCOPY Dmax: 113.4 Å Quality: EXCELLENT

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

DNA polymerase epsilon subunit B

Saccharomyces cerevisiae

UniProt P24482

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 B; UniProt 1–689 Not recorded DNA polymerase epsilon catalytic subunit A × 1 (P21951) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPB2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–689; UniProt 1–689

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1308–2221 Not recorded DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

33 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–914; UniProt 1308–2221

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 6hv8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6hv8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6hv8
Deposition date deposition_date2018-10-10
Structure title titleCryo-EM structure of S. cerevisiae Polymerase epsilon deltacat mutant
Keywords keywordsPolymerase epsilon, DNA replication, enzyme, DNA polymerase, 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_guinier36.72
Radius of gyration Rg (electron density) rg_electron35.69
Forward intensity I(0) i0253189000.00
Molecular weight molecular_weight130790.0 kDa
Excluded volume excluded_volume165020 ų
Envelope volume envelope_volume244880 ų
Hydration-shell volume shell_volume56504 ų
Envelope diameter envelope_diameter114.9
Shell Rg shell_rg42.77
Envelope Rg envelope_rg35.22
Shape Rg shape_rg35.69
Total Rg total_rg36.27
Total atoms total_atoms9206
Residues n_residues1184
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 dmax113.4
Rg (real space) rg_real36.53
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real2.5320e+08
I(0) uncertainty (real space) i0_real_error3.6880e+06
Rg (reciprocal space) rg_reciprocal36.65
I(0) (reciprocal space) i0_reciprocal253200000.0000
Solution quality estimate total_estimate0.9078
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.5
Skewness Skewness skewness0.132
Kurtosis Kurtosis kurtosis-0.597
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64660000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)