9y4c

Strand displacement state I of Human mitochondrial DNA polymerase gamma ternary complex

Method: ELECTRON MICROSCOPY Dmax: 143.6 Å Quality: GOOD

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

DNA polymerase subunit gamma-1

Homo sapiens

UniProt P54098

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 × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–1239 Mutation:D198A, E200A DNA polymerase subunit gamma-2, mitochondrial × 2 (Q9UHN1) DNA (77-MER) × 1 CA CALCIUM ION × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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.

35 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1239; UniProt 1–1239

DNA polymerase subunit gamma-2, mitochondrial

Homo sapiens

UniProt Q9UHN1

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 × 3 DNA 1 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 1–485 Chain C; UniProt 1–485 Not recorded DNA polymerase subunit gamma-1 × 1 (P54098) DNA (77-MER) × 1 CA CALCIUM ION × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.23 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.

36 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–485; UniProt 1–485 Author chain C; PDBConstruct 1–485; UniProt 1–485

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 9y4c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y4c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y4c
Deposition date deposition_date2025-09-03
Structure title titleStrand displacement state I of Human mitochondrial DNA polymerase gamma ternary complex
Keywords keywordsDNA polymerase gamma, strand displacement, mitochondria, TRANSFERASE-DNA complex; TRANSFERASE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.22
Radius of gyration Rg (electron density) rg_electron42.97
Forward intensity I(0) i0789266000.00
Molecular weight molecular_weight218800.0 kDa
Excluded volume excluded_volume268650 ų
Envelope volume envelope_volume401120 ų
Hydration-shell volume shell_volume76441 ų
Envelope diameter envelope_diameter157.9
Shell Rg shell_rg49.14
Envelope Rg envelope_rg42.41
Shape Rg shape_rg42.99
Total Rg total_rg43.21
Total atoms total_atoms15330
Residues n_residues1813
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 dmax143.6
Rg (real space) rg_real43.19
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real7.8930e+08
I(0) uncertainty (real space) i0_real_error1.3630e+07
Rg (reciprocal space) rg_reciprocal43.22
I(0) (reciprocal space) i0_reciprocal789300000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.240
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha164500000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.811

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)