8var

Structure of the E. coli clamp loader bound to the beta clamp in a Closed-DNA2 conformation

Method: ELECTRON MICROSCOPY Dmax: 132.2 Å Quality: GOOD

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

DNA polymerase III subunit delta

Escherichia coli

UniProt P28630

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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain A; UniProt 1–343 Not recorded DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) Beta sliding clamp × 2 (P0A988) ;DNA (5'-D(P*GP*CP*AP*GP*AP*CP*AP*CP*TP*AP*CP*GP*AP*GP*TP*AP*CP*AP*TP*A)-3') ; × 1 DNA (27-MER) × 1 ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 BEF BERYLLIUM TRIFLUORIDE ION × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLA_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–343; UniProt 1–343

DNA polymerase III subunit tau

Escherichia coli

UniProt P06710

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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain B; UniProt 1–373 Chain C; UniProt 1–373 Chain D; UniProt 1–373 Not recorded DNA polymerase III subunit delta × 1 (P28630) ;DNA polymerase III subunit delta' ; × 1 (P28631) Beta sliding clamp × 2 (P0A988) ;DNA (5'-D(P*GP*CP*AP*GP*AP*CP*AP*CP*TP*AP*CP*GP*AP*GP*TP*AP*CP*AP*TP*A)-3') ; × 1 DNA (27-MER) × 1 ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 BEF BERYLLIUM TRIFLUORIDE ION × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

38 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3X_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–376; UniProt 1–373 Author chain C; PDBConstruct 4–376; UniProt 1–373 Author chain D; PDBConstruct 4–376; UniProt 1–373

;DNA polymerase III subunit delta' ;

Escherichia coli

UniProt P28631

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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain E; UniProt 1–334 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) Beta sliding clamp × 2 (P0A988) ;DNA (5'-D(P*GP*CP*AP*GP*AP*CP*AP*CP*TP*AP*CP*GP*AP*GP*TP*AP*CP*AP*TP*A)-3') ; × 1 DNA (27-MER) × 1 ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 BEF BERYLLIUM TRIFLUORIDE ION × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

34 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLB_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 4–337; UniProt 1–334

Beta sliding clamp

Escherichia coli

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 × 7 DNA 2 PDB declaration: nonameric(9) Consistent with all polymer counts Chain F; UniProt 1–366 Chain G; UniProt 1–366 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) ;DNA (5'-D(P*GP*CP*AP*GP*AP*CP*AP*CP*TP*AP*CP*GP*AP*GP*TP*AP*CP*AP*TP*A)-3') ; × 1 DNA (27-MER) × 1 ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 3 BEF BERYLLIUM TRIFLUORIDE ION × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 4
Chains and sequence ranges Author chain F; PDBConstruct 4–369; UniProt 1–366 Author chain G; PDBConstruct 4–369; UniProt 1–366

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 8var

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8var
Deposition date deposition_date2023-12-11
Structure title titleStructure of the E. coli clamp loader bound to the beta clamp in a Closed-DNA2 conformation
Keywords keywordsBacterial Clamp Loader Complex, REPLICATION, TRANSFERASE-DNA complex, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.04
Radius of gyration Rg (electron density) rg_electron42.61
Forward intensity I(0) i01372530000.00
Molecular weight molecular_weight294450.0 kDa
Excluded volume excluded_volume363860 ų
Envelope volume envelope_volume501910 ų
Hydration-shell volume shell_volume92728 ų
Envelope diameter envelope_diameter141.1
Shell Rg shell_rg52.13
Envelope Rg envelope_rg41.50
Shape Rg shape_rg42.62
Total Rg total_rg42.97
Total atoms total_atoms20590
Residues n_residues2551
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 dmax132.2
Rg (real space) rg_real42.78
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.3730e+09
I(0) uncertainty (real space) i0_real_error2.2560e+07
Rg (reciprocal space) rg_reciprocal43.04
I(0) (reciprocal space) i0_reciprocal1373000000.0000
Solution quality estimate total_estimate0.8906
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.6
Skewness Skewness skewness0.120
Kurtosis Kurtosis kurtosis-0.482
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239500000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)