5fkw

cryo-EM structure of the E. coli replicative DNA polymerase complex bound to DNA (DNA polymerase III alpha, beta, epsilon)

Method: ELECTRON MICROSCOPY Dmax: 139.7 Å Quality: GOOD

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

DNA POLYMERASE III ALPHA

ESCHERICHIA COLI K-12

UniProt P10443

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–1160 Mutation:YES DNA POLYMERASE III BETA × 2 (P0A988) DNA POLYMERASE III EPSILON × 1 (P03007) PRIMER-TEMPLATE DUPLEX DNA × 1 PRIMER-TEMPLATE DUPLEX DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT;pH 7.5;25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.30 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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3A_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1160; UniProt 1–1160

DNA POLYMERASE III BETA

ESCHERICHIA COLI K-12

UniProt P0A988

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–366 Chain C; UniProt 1–366 Not recorded DNA POLYMERASE III ALPHA × 1 (P10443) DNA POLYMERASE III EPSILON × 1 (P03007) PRIMER-TEMPLATE DUPLEX DNA × 1 PRIMER-TEMPLATE DUPLEX DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT;pH 7.5;25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.30 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.

53 other PDB entries and 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3B_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–366; UniProt 1–366 Author chain C; PDBConstruct 1–366; UniProt 1–366

DNA POLYMERASE III EPSILON

ESCHERICHIA COLI K-12

UniProt P03007

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 1–243 Mutation:YES DNA POLYMERASE III ALPHA × 1 (P10443) DNA POLYMERASE III BETA × 2 (P0A988) PRIMER-TEMPLATE DUPLEX DNA × 1 PRIMER-TEMPLATE DUPLEX DNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT;pH 7.5;25 MM HEPES PH 7.5, 150 MM NACL, AND 2 MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.30 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.

10 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3E_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–243; UniProt 1–243

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 5fkw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fkw
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5fkw
Deposition date deposition_date2015-10-20
Structure title titlecryo-EM structure of the E. coli replicative DNA polymerase complex bound to DNA (DNA polymerase III alpha, beta, epsilon)
Keywords keywordsTRANSFERASE, DNA REPLICATION, DNA POLYMERASE III ALPHA, DNA POLYMERASE III BETA, DNA POLYMERASE III EPSILON; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.79
Radius of gyration Rg (electron density) rg_electron43.92
Forward intensity I(0) i0814276000.00
Molecular weight molecular_weight224760.0 kDa
Excluded volume excluded_volume276970 ų
Envelope volume envelope_volume401220 ų
Hydration-shell volume shell_volume75284 ų
Envelope diameter envelope_diameter140.9
Shell Rg shell_rg50.19
Envelope Rg envelope_rg42.34
Shape Rg shape_rg43.95
Total Rg total_rg44.09
Total atoms total_atoms15726
Residues n_residues1929
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_real43.64
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real8.1430e+08
I(0) uncertainty (real space) i0_real_error1.4120e+07
Rg (reciprocal space) rg_reciprocal43.79
I(0) (reciprocal space) i0_reciprocal814400000.0000
Solution quality estimate total_estimate0.8905
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.3
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.476
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha108600000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.813

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)