9oyh

Structure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 1 the DNA recognition state

Method: ELECTRON MICROSCOPY Dmax: 151.0 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 × 9 DNA 2 PDB declaration: 11-meric(11) 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 (P0A990) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit psi × 1 (P28632) DNA polymerase III subunit chi × 1 (P28905) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts 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) Beta sliding clamp × 2 (P0A990) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit psi × 1 (P28632) DNA polymerase III subunit chi × 1 (P28905) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) 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 (P0A990) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit psi × 1 (P28632) DNA polymerase III subunit chi × 1 (P28905) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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

Beta sliding clamp

Escherichia coli

UniProt P0A990

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 × 9 DNA 2 PDB declaration: 11-meric(11) 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) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit psi × 1 (P28632) DNA polymerase III subunit chi × 1 (P28905) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPO3B_ECO57
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–366; UniProt 1–366 Author chain G; PDBConstruct 1–366; UniProt 1–366

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–DNA Heteromer Protein × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain J; UniProt 1–137 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) Beta sliding clamp × 2 (P0A990) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit chi × 1 (P28905) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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 7
Chains and sequence ranges Author chain J; PDBConstruct 1–137; UniProt 1–137

DNA polymerase III subunit chi

Escherichia coli

UniProt P28905

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 × 9 DNA 2 PDB declaration: 11-meric(11) Consistent with all polymer counts Chain L; UniProt 2–147 Not recorded DNA polymerase III subunit delta × 1 (P28630) DNA polymerase III subunit tau × 3 (P06710) ;DNA polymerase III subunit delta' ; × 1 (P28631) Beta sliding clamp × 2 (P0A990) 10-nt gapped DNA template strand × 1 10-nt gapped DNA primer strand 1 × 1 DNA polymerase III subunit psi × 1 (P28632) ZN ZINC ION × 4 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HOLC_ECOLI
Isoform
PDB entities 8
Chains and sequence ranges Author chain L; PDBConstruct 1–146; UniProt 2–147

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 9oyh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oyh
Deposition date deposition_date2025-06-04
Structure title titleStructure of the E. coli clamp loader DnaX-complex loading beta-clamp onto 10-nt gapped DNA in state 1 the DNA recognition state
Keywords keywords;DNA replication, DNA damage repair, clamp loading complex, clamp beta, clamp loader DnaX-complex, REPLICATION, 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_guinier47.91
Radius of gyration Rg (electron density) rg_electron47.44
Forward intensity I(0) i01640650000.00
Molecular weight molecular_weight324360.0 kDa
Excluded volume excluded_volume401370 ų
Envelope volume envelope_volume577710 ų
Hydration-shell volume shell_volume99128 ų
Envelope diameter envelope_diameter161.3
Shell Rg shell_rg54.14
Envelope Rg envelope_rg46.58
Shape Rg shape_rg47.47
Total Rg total_rg47.58
Total atoms total_atoms22701
Residues n_residues2823
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 dmax151.0
Rg (real space) rg_real47.74
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real1.6410e+09
I(0) uncertainty (real space) i0_real_error3.0420e+07
Rg (reciprocal space) rg_reciprocal47.91
I(0) (reciprocal space) i0_reciprocal1641000000.0000
Solution quality estimate total_estimate0.8488
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.304
Kurtosis Kurtosis kurtosis-0.102
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha147700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.491

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)