3ikm

Crystal structure of human mitochondrial DNA polymerase holoenzyme

Method: X-RAY DIFFRACTION Dmax: 193.0 Å Quality: GOOD

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

DNA polymerase subunit gamma-1

OrganismNot specified

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 70–1239 Fragment:UNP residues 70-1239 DNA polymerase subunit gamma-2 × 2 (Q9UHN1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;VAPOR DIFFUSION Resolution 3.24 Å R-free 0.303
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 70–1239 Fragment:UNP residues 70-1239 DNA polymerase subunit gamma-2 × 2 (Q9UHN1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;VAPOR DIFFUSION Resolution 3.24 Å R-free 0.303

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 35 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 1–1172; UniProt 70–1239 Author chain D; PDBConstruct 1–1172; UniProt 70–1239

DNA polymerase subunit gamma-2

OrganismNot specified

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 59–485 Chain C; UniProt 59–485 Fragment:UNP residues 59-485 DNA polymerase subunit gamma-1 × 1 (P54098) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;VAPOR DIFFUSION Resolution 3.24 Å R-free 0.303
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 59–485 Chain F; UniProt 59–485 Fragment:UNP residues 59-485 DNA polymerase subunit gamma-1 × 1 (P54098) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;VAPOR DIFFUSION Resolution 3.24 Å R-free 0.303

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 37 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 1–427; UniProt 59–485 Author chain C; PDBConstruct 1–427; UniProt 59–485 Author chain E; PDBConstruct 1–427; UniProt 59–485 Author chain F; PDBConstruct 1–427; UniProt 59–485

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 3ikm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ikm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ikm
Deposition date deposition_date2009-08-06
Structure title titleCrystal structure of human mitochondrial DNA polymerase holoenzyme
Keywords keywords;Human mitochondrial DNA polymerase, Disease mutation, DNA replication, DNA-binding, DNA-directed DNA polymerase, Magnesium, Mitochondrion, Neuropathy, Nucleotidyltransferase, Progressive external ophthalmoplegia, Transferase, Transit peptide ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.20
Radius of gyration Rg (electron density) rg_electron57.77
Forward intensity I(0) i02468210000.00
Molecular weight molecular_weight418480.0 kDa
Excluded volume excluded_volume523960 ų
Envelope volume envelope_volume781830 ų
Hydration-shell volume shell_volume110990 ų
Envelope diameter envelope_diameter194.1
Shell Rg shell_rg61.92
Envelope Rg envelope_rg55.87
Shape Rg shape_rg57.77
Total Rg total_rg57.87
Total atoms total_atoms29480
Residues n_residues3689
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 dmax193.0
Rg (real space) rg_real58.06
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real2.4680e+09
I(0) uncertainty (real space) i0_real_error4.7110e+07
Rg (reciprocal space) rg_reciprocal58.28
I(0) (reciprocal space) i0_reciprocal2469000000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.5
Skewness Skewness skewness0.155
Kurtosis Kurtosis kurtosis-0.677
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha276200000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 11 domains

CATH v4.4 (11 domains)

Domain ID domain_id3ikmA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily390
Domain ID domain_id3ikmA04
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily3960
Domain ID domain_id3ikmB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id3ikmB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily800 — Anticodon-binding domain
Domain ID domain_id3ikmC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id3ikmC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily800 — Anticodon-binding domain
Domain ID domain_id3ikmD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily390
Domain ID domain_id3ikmE01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id3ikmE02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily800 — Anticodon-binding domain
Domain ID domain_id3ikmF01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily10 — Bira Bifunctional Protein; Domain 2
Domain ID domain_id3ikmF02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily800 — Anticodon-binding domain

8. Citations (1)

9. Files and Curves (10)