8d33

Human mitochondrial DNA polymerase gamma ternary complex with GC basepair

Method: ELECTRON MICROSCOPY Dmax: 139.2 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 1–1239 Not recorded DNA polymerase subunit gamma-2, mitochondrial × 2 (Q9UHN1) ;DNA (5'-D(P*AP*AP*AP*AP*CP*GP*AP*CP*GP*GP*CP*CP*AP*GP*TP*GP*CP*CP*AP*TP*AP*C)-3') ; × 1 DNA (25-MER) × 1 CA CALCIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.46 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 2 PDB declaration: pentameric(5) 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 (5'-D(P*AP*AP*AP*AP*CP*GP*AP*CP*GP*GP*CP*CP*AP*GP*TP*GP*CP*CP*AP*TP*AP*C)-3') ; × 1 DNA (25-MER) × 1 CA CALCIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.46 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 8d33

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d33
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d33
Deposition date deposition_date2022-05-31
Structure title titleHuman mitochondrial DNA polymerase gamma ternary complex with GC basepair
Keywords keywordsDNA-binding protein, DNA polymerase, 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_guinier42.14
Radius of gyration Rg (electron density) rg_electron41.90
Forward intensity I(0) i0759188000.00
Molecular weight molecular_weight217750.0 kDa
Excluded volume excluded_volume268760 ų
Envelope volume envelope_volume377850 ų
Hydration-shell volume shell_volume73470 ų
Envelope diameter envelope_diameter142.9
Shell Rg shell_rg48.35
Envelope Rg envelope_rg41.48
Shape Rg shape_rg41.90
Total Rg total_rg42.19
Total atoms total_atoms15272
Residues n_residues1830
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 dmax139.2
Rg (real space) rg_real42.08
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real7.5920e+08
I(0) uncertainty (real space) i0_real_error1.3400e+07
Rg (reciprocal space) rg_reciprocal42.14
I(0) (reciprocal space) i0_reciprocal759200000.0000
Solution quality estimate total_estimate0.8847
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.9
Skewness Skewness skewness0.304
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha121400000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.875

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)