9p4j

The structure of Retron Eco8 in Apo state

Method: ELECTRON MICROSCOPY Dmax: 221.9 Å Quality: GOOD

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

Retron Eco8 OLD nuclease

Escherichia coli

UniProt P0DV58

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 DNA 4 RNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain A; UniProt 1–750 Chain B; UniProt 1–750 Chain C; UniProt 1–750 Chain D; UniProt 1–750 Not recorded Retron Eco8 reverse transcriptase × 4 (P0DV59) msrRNA × 4 msdDNA × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.68 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OLD8_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–750; UniProt 1–750 Author chain B; PDBConstruct 1–750; UniProt 1–750 Author chain C; PDBConstruct 1–750; UniProt 1–750 Author chain D; PDBConstruct 1–750; UniProt 1–750

Retron Eco8 reverse transcriptase

Escherichia coli

UniProt P0DV59

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 DNA 4 RNA 4 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain E; UniProt 2–374 Chain F; UniProt 2–374 Chain G; UniProt 2–374 Chain H; UniProt 2–374 Not recorded Retron Eco8 OLD nuclease × 4 (P0DV58) msrRNA × 4 msdDNA × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.68 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RT8_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–373; UniProt 2–374 Author chain F; PDBConstruct 1–373; UniProt 2–374 Author chain G; PDBConstruct 1–373; UniProt 2–374 Author chain H; PDBConstruct 1–373; UniProt 2–374

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 9p4j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9p4j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9p4j
Deposition date deposition_date2025-06-16
Structure title titleThe structure of Retron Eco8 in Apo state
Keywords keywordsanti-phage, bacterial immunity, retron, DNA, RNA, reverse transcription, Transferase-Hydrolase-DNA-RNA complex; Transferase/Hydrolase/DNA/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.66
Radius of gyration Rg (electron density) rg_electron62.85
Forward intensity I(0) i08613140000.00
Molecular weight molecular_weight681850.0 kDa
Excluded volume excluded_volume810050 ų
Envelope volume envelope_volume1327800 ų
Hydration-shell volume shell_volume169280 ų
Envelope diameter envelope_diameter236.8
Shell Rg shell_rg68.66
Envelope Rg envelope_rg61.79
Shape Rg shape_rg62.73
Total Rg total_rg63.31
Total atoms total_atoms47375
Residues n_residues4960
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 dmax221.9
Rg (real space) rg_real65.39
Rg uncertainty (real space) rg_real_error2.27
I(0) (real space) i0_real8.6130e+09
I(0) uncertainty (real space) i0_real_error1.7760e+08
Rg (reciprocal space) rg_reciprocal65.85
I(0) (reciprocal space) i0_reciprocal8620000000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary74.0
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha818900000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)