9trl

RAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (beta-barrel)

Method: ELECTRON MICROSCOPY Dmax: 150.7 Å Quality: GOOD

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

DNA repair protein RAD51 homolog 1

Homo

UniProt Q06609

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 × 11 DNA 1 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain A; UniProt 1–339 Chain B; UniProt 1–339 Chain C; UniProt 1–339 Chain D; UniProt 1–339 Chain E; UniProt 1–339 Chain F; UniProt 1–339 Not recorded DNA repair and recombination protein RAD54B × 4 (Q9Y620) DNA repair and recombination protein RAD54B × 1 (Q9Y620) DNA × 1 K POTASSIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

50 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD51_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–339; UniProt 1–339 Author chain B; PDBConstruct 1–339; UniProt 1–339 Author chain C; PDBConstruct 1–339; UniProt 1–339 Author chain D; PDBConstruct 1–339; UniProt 1–339 Author chain E; PDBConstruct 1–339; UniProt 1–339 Author chain F; PDBConstruct 1–339; UniProt 1–339

DNA repair and recombination protein RAD54B

Homo sapiens

UniProt Q9Y620

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 × 11 DNA 1 PDB declaration: 12-meric(12) Consistent with all polymer counts Chain H; UniProt 1–285 Chain I; UniProt 1–285 Chain J; UniProt 1–285 Chain K; UniProt 1–285 Chain O; UniProt 1–285 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA repair protein RAD51 homolog 1 × 6 (Q06609) DNA × 1 K POTASSIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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

View Construct and Data Evidence
UniProt name RA54B_HUMAN
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain H; PDBConstruct 2–286; UniProt 1–285 Author chain I; PDBConstruct 2–286; UniProt 1–285 Author chain J; PDBConstruct 2–286; UniProt 1–285 Author chain K; PDBConstruct 2–286; UniProt 1–285 Author chain O; PDBConstruct 1–285; UniProt 1–285

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 9trl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9trl
Deposition date deposition_date2025-12-25
Structure title titleRAD51-ssDNA filament in complex with magnesium and ATP bound by the RAD54B N-terminus (beta-barrel)
Keywords keywordsRAD51 recombinase, RAD54B, filament modulation, homologous recombination, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.98
Radius of gyration Rg (electron density) rg_electron44.90
Forward intensity I(0) i0854023000.00
Molecular weight molecular_weight231950.0 kDa
Excluded volume excluded_volume286680 ų
Envelope volume envelope_volume395710 ų
Hydration-shell volume shell_volume72272 ų
Envelope diameter envelope_diameter159.0
Shell Rg shell_rg50.45
Envelope Rg envelope_rg44.38
Shape Rg shape_rg44.92
Total Rg total_rg45.07
Total atoms total_atoms16206
Residues n_residues2051
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 dmax150.7
Rg (real space) rg_real45.02
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real8.5400e+08
I(0) uncertainty (real space) i0_real_error1.7270e+07
Rg (reciprocal space) rg_reciprocal44.99
I(0) (reciprocal space) i0_reciprocal854000000.0000
Solution quality estimate total_estimate0.8755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.1
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha281200000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.796

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)