9oyg

Structure of the E. coli clamp loader DnaX-complex alone

Method: ELECTRON MICROSCOPY Dmax: 123.3 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–343 Not recorded DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) DNA polymerase III subunit psi × 1 (P28632) ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–643 Chain C; UniProt 1–643 Chain D; UniProt 1–643 Not recorded DNA polymerase III subunit delta × 1 (P28630) ;DNA polymerase III subunit delta' ; × 1 (P28631) DNA polymerase III subunit psi × 1 (P28632) ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 1–643; UniProt 1–643 Author chain C; PDBConstruct 1–643; UniProt 1–643 Author chain D; PDBConstruct 1–643; UniProt 1–643

;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 heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–334 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) DNA polymerase III subunit psi × 1 (P28632) ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 1–334; UniProt 1–334

DNA polymerase III subunit psi

Escherichia coli

UniProt P28632

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain J; UniProt 3–32 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) ZN ZINC ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLD_ECOLI
Isoform
PDB entities 4
Chains and sequence ranges Author chain J; PDBConstruct 1–30; UniProt 3–32

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 9oyg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9oyg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9oyg
Deposition date deposition_date2025-06-04
Structure title titleStructure of the E. coli clamp loader DnaX-complex alone
Keywords keywordsDNA replication, DNA damage repair, clamp loading complex, clamp beta, clamp loader DnaX-complex, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.78
Radius of gyration Rg (electron density) rg_electron39.74
Forward intensity I(0) i0617059000.00
Molecular weight molecular_weight201170.0 kDa
Excluded volume excluded_volume251500 ų
Envelope volume envelope_volume357570 ų
Hydration-shell volume shell_volume72899 ų
Envelope diameter envelope_diameter122.8
Shell Rg shell_rg47.90
Envelope Rg envelope_rg38.03
Shape Rg shape_rg39.74
Total Rg total_rg40.19
Total atoms total_atoms14137
Residues n_residues1794
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 dmax123.3
Rg (real space) rg_real40.53
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real6.1710e+08
I(0) uncertainty (real space) i0_real_error9.1570e+06
Rg (reciprocal space) rg_reciprocal40.78
I(0) (reciprocal space) i0_reciprocal617200000.0000
Solution quality estimate total_estimate0.9047
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.9
Skewness Skewness skewness-0.009
Kurtosis Kurtosis kurtosis-0.632
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75530000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)