7qo1

complex of DNA ligase I and FEN1 on PCNA and DNA

Method: ELECTRON MICROSCOPY Dmax: 121.8 Å Quality: GOOD

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

DNA ligase 1

Homo sapiens

UniProt P18858

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 × 5 DNA 3 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 161–919 Not recorded Proliferating cell nuclear antigen × 3 (P12004) Oligo19ddC × 1 Oligo13P × 1 Oligo32 × 1 Flap endonuclease 1 × 1 (P39748) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNLI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–760; UniProt 161–919

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 × 5 DNA 3 PDB declaration: octameric(8) Consistent with all polymer counts Chain B; UniProt 1–261 Chain F; UniProt 1–261 Chain G; UniProt 1–261 Not recorded DNA ligase 1 × 1 (P18858) Oligo19ddC × 1 Oligo13P × 1 Oligo32 × 1 Flap endonuclease 1 × 1 (P39748) AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

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 4–264; UniProt 1–261 Author chain F; PDBConstruct 4–264; UniProt 1–261 Author chain G; PDBConstruct 4–264; UniProt 1–261

Flap endonuclease 1

Homo sapiens

UniProt P39748

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 × 5 DNA 3 PDB declaration: octameric(8) Consistent with all polymer counts Chain Y; UniProt 1–380 Mutation:D181A DNA ligase 1 × 1 (P18858) Proliferating cell nuclear antigen × 3 (P12004) Oligo19ddC × 1 Oligo13P × 1 Oligo32 × 1 AMP ADENOSINE MONOPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 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.

26 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEN1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain Y; PDBConstruct 1–380; UniProt 1–380

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 7qo1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qo1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qo1
Deposition date deposition_date2021-12-23
Structure title titlecomplex of DNA ligase I and FEN1 on PCNA and DNA
Keywords keywordsDNA, Replication, Complex, Ligase, PCNA, Ligation, FEN1, Flap Endonuclease I, Okazaki fragment maturation; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.32
Radius of gyration Rg (electron density) rg_electron40.93
Forward intensity I(0) i0696494000.00
Molecular weight molecular_weight203170.0 kDa
Excluded volume excluded_volume248800 ų
Envelope volume envelope_volume367000 ų
Hydration-shell volume shell_volume72540 ų
Envelope diameter envelope_diameter126.7
Shell Rg shell_rg48.68
Envelope Rg envelope_rg39.59
Shape Rg shape_rg40.95
Total Rg total_rg41.27
Total atoms total_atoms14179
Residues n_residues1755
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 dmax121.8
Rg (real space) rg_real41.09
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real6.9650e+08
I(0) uncertainty (real space) i0_real_error1.1820e+07
Rg (reciprocal space) rg_reciprocal41.31
I(0) (reciprocal space) i0_reciprocal696700000.0000
Solution quality estimate total_estimate0.8918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.5
Skewness Skewness skewness0.050
Kurtosis Kurtosis kurtosis-0.604
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85870000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.682

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)