9f6j

Human DNA Polymerase epsilon bound to T-C mismatched DNA (Polymerase Arrest state)

Method: ELECTRON MICROSCOPY Dmax: 107.5 Å Quality: REASONABLE

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

DNA polymerase epsilon catalytic subunit A

Homo sapiens

UniProt Q07864

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 1–1200 Not recorded DNA nascent strand × 1 DNA template strand × 1 SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

16 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1200; UniProt 1–1200

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 9f6j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f6j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f6j
Deposition date deposition_date2024-05-01
Structure title titleHuman DNA Polymerase epsilon bound to T-C mismatched DNA (Polymerase Arrest state)
Keywords keywordsDNA, polymerase, epsilon, PCNA, leading strand, human, replication, replisome, proofreading; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.81
Radius of gyration Rg (electron density) rg_electron35.07
Forward intensity I(0) i0321957000.00
Molecular weight molecular_weight139300.0 kDa
Excluded volume excluded_volume172140 ų
Envelope volume envelope_volume248780 ų
Hydration-shell volume shell_volume57440 ų
Envelope diameter envelope_diameter109.6
Shell Rg shell_rg43.10
Envelope Rg envelope_rg34.24
Shape Rg shape_rg35.07
Total Rg total_rg35.64
Total atoms total_atoms9751
Residues n_residues1150
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 dmax107.5
Rg (real space) rg_real35.55
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real3.2200e+08
I(0) uncertainty (real space) i0_real_error5.1450e+06
Rg (reciprocal space) rg_reciprocal35.71
I(0) (reciprocal space) i0_reciprocal322000000.0000
Solution quality estimate total_estimate0.6981
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.4
Skewness Skewness skewness0.038
Kurtosis Kurtosis kurtosis-0.579
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40230000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.971; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)