9ne8

Human polymerase epsilon bound to PCNA and DNA with an in-situ-generated mismatch in the mismatch-locking state

Method: ELECTRON MICROSCOPY Dmax: 132.9 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 Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–1200 Not recorded Proliferating cell nuclear antigen × 3 (P12004) DNA (33-MER) × 1 DNA (47-MER) × 1 SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 (33-MER) × 1 DNA (47-MER) × 1 SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 9ne8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ne8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ne8
Deposition date deposition_date2025-02-19
最后修订 last_revision2025-06-04
Structure title titleHuman polymerase epsilon bound to PCNA and DNA with an in-situ-generated mismatch in the mismatch-locking state
Keywords keywordsDNA polymerase, exo, holoenzyme, DNA, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.40
Radius of gyration Rg (electron density) rg_electron42.12
Forward intensity I(0) i0858489000.00
Molecular weight molecular_weight232400.0 kDa
Excluded volume excluded_volume287120 ų
Envelope volume envelope_volume410300 ų
Hydration-shell volume shell_volume79009 ų
Envelope diameter envelope_diameter137.0
Shell Rg shell_rg49.44
Envelope Rg envelope_rg40.92
Shape Rg shape_rg42.13
Total Rg total_rg42.42
Total atoms total_atoms16242
Residues n_residues1967
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 dmax132.9
Rg (real space) rg_real42.24
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real8.5850e+08
I(0) uncertainty (real space) i0_real_error1.3220e+07
Rg (reciprocal space) rg_reciprocal42.40
I(0) (reciprocal space) i0_reciprocal858600000.0000
Solution quality estimate total_estimate0.6015
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.3
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha122600000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 0.016; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)