8v55

Human mitochondrial DNA polymerase gamma bound to a replication fork in an open conformation

Method: ELECTRON MICROSCOPY Dmax: 139.7 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 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 26–1239 Mutation:D198A, E200A DNA polymerase subunit gamma-2, mitochondrial × 2 (Q9UHN1) DNA primer chain × 1 DNA template chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 16–1229; UniProt 26–1239

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 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain B; UniProt 26–485 Chain C; UniProt 26–485 Not recorded DNA polymerase subunit gamma-1 × 1 (P54098) DNA primer chain × 1 DNA template chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 15–474; UniProt 26–485 Author chain C; PDBConstruct 15–474; UniProt 26–485

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 8v55

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v55
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v55
Deposition date deposition_date2023-11-30
Structure title titleHuman mitochondrial DNA polymerase gamma bound to a replication fork in an open conformation
Keywords keywordsDNA BINDING PROTEIN, DNA polymerase, mitochondrial DNA replication, DNA polymerase gamma, DNA BINDING PROTEIN-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.30
Radius of gyration Rg (electron density) rg_electron42.66
Forward intensity I(0) i0691788000.00
Molecular weight molecular_weight207900.0 kDa
Excluded volume excluded_volume256610 ų
Envelope volume envelope_volume369780 ų
Hydration-shell volume shell_volume70851 ų
Envelope diameter envelope_diameter136.5
Shell Rg shell_rg48.90
Envelope Rg envelope_rg41.90
Shape Rg shape_rg42.64
Total Rg total_rg43.01
Total atoms total_atoms14582
Residues n_residues1754
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 dmax139.7
Rg (real space) rg_real43.19
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real6.9180e+08
I(0) uncertainty (real space) i0_real_error1.2530e+07
Rg (reciprocal space) rg_reciprocal43.30
I(0) (reciprocal space) i0_reciprocal691900000.0000
Solution quality estimate total_estimate0.8296
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80560000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)