9x94

Apo Retron-Eco8 complex

Method: ELECTRON MICROSCOPY Dmax: 219.0 Å Quality: REASONABLE

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

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 A; UniProt 1–374 Chain E; UniProt 1–374 Chain I; UniProt 1–374 Chain M; UniProt 1–374 Not recorded Retron Eco8 OLD nuclease × 4 (P0DV58) RNA (81-MER) × 4 DNA (75-MER) × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–374; UniProt 1–374 Author chain E; PDBConstruct 1–374; UniProt 1–374 Author chain I; PDBConstruct 1–374; UniProt 1–374 Author chain M; PDBConstruct 1–374; UniProt 1–374

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 B; UniProt 1–750 Chain F; UniProt 1–750 Chain J; UniProt 1–750 Chain N; UniProt 1–750 Not recorded Retron Eco8 reverse transcriptase × 4 (P0DV59) RNA (81-MER) × 4 DNA (75-MER) × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–750; UniProt 1–750 Author chain F; PDBConstruct 1–750; UniProt 1–750 Author chain J; PDBConstruct 1–750; UniProt 1–750 Author chain N; PDBConstruct 1–750; UniProt 1–750

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 9x94

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x94
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x94
Deposition date deposition_date2025-10-20
Structure title titleApo Retron-Eco8 complex
Keywords keywordscomplex, RNA BINDING PROTEIN/RNA/DNA, RNA BINDING PROTEIN-RNA-DNA complex; RNA BINDING PROTEIN/RNA/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.60
Radius of gyration Rg (electron density) rg_electron62.17
Forward intensity I(0) i07160440000.00
Molecular weight molecular_weight644350.0 kDa
Excluded volume excluded_volume776790 ų
Envelope volume envelope_volume1275200 ų
Hydration-shell volume shell_volume164150 ų
Envelope diameter envelope_diameter230.1
Shell Rg shell_rg67.83
Envelope Rg envelope_rg61.40
Shape Rg shape_rg62.05
Total Rg total_rg62.65
Total atoms total_atoms86096
Residues n_residues4818
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 dmax219.0
Rg (real space) rg_real64.40
Rg uncertainty (real space) rg_real_error2.35
I(0) (real space) i0_real7.1600e+09
I(0) uncertainty (real space) i0_real_error1.5010e+08
Rg (reciprocal space) rg_reciprocal64.75
I(0) (reciprocal space) i0_reciprocal7165000000.0000
Solution quality estimate total_estimate0.6379
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary82.1
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.339
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha720000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.972; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)