9f6f

Human DNA polymerase epsilon bound to DNA and PCNA (closed conformation)

Method: ELECTRON MICROSCOPY Dmax: 135.8 Å Quality: GOOD

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 Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–1200 Mutation:D275A E277A Proliferating cell nuclear antigen × 3 (P12004) DNA nascent strand × 1 DNA template strand × 1 SF4 IRON/SULFUR CLUSTER × 1 DDS 2',3'-dideoxyadenosine triphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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

Proliferating cell nuclear antigen

Homo sapiens

UniProt P12004

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 Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–261 Chain C; UniProt 1–261 Chain D; UniProt 1–261 Not recorded DNA polymerase epsilon catalytic subunit A × 1 (Q07864) DNA nascent strand × 1 DNA template strand × 1 SF4 IRON/SULFUR CLUSTER × 1 DDS 2',3'-dideoxyadenosine triphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

101 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–261; UniProt 1–261 Author chain C; PDBConstruct 1–261; UniProt 1–261 Author chain D; PDBConstruct 1–261; UniProt 1–261

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 9f6f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f6f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f6f
Deposition date deposition_date2024-05-01
Structure title titleHuman DNA polymerase epsilon bound to DNA and PCNA (closed conformation)
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_guinier43.44
Radius of gyration Rg (electron density) rg_electron43.18
Forward intensity I(0) i0887333000.00
Molecular weight molecular_weight234470.0 kDa
Excluded volume excluded_volume288870 ų
Envelope volume envelope_volume433690 ų
Hydration-shell volume shell_volume81562 ų
Envelope diameter envelope_diameter140.7
Shell Rg shell_rg50.36
Envelope Rg envelope_rg41.78
Shape Rg shape_rg43.19
Total Rg total_rg43.46
Total atoms total_atoms16376
Residues n_residues1969
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 dmax135.8
Rg (real space) rg_real43.26
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real8.8730e+08
I(0) uncertainty (real space) i0_real_error1.5910e+07
Rg (reciprocal space) rg_reciprocal43.44
I(0) (reciprocal space) i0_reciprocal887500000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.8
Skewness Skewness skewness0.181
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha136200000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)