9tyy

RAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54 N-terminus

Method: ELECTRON MICROSCOPY Dmax: 146.9 Å Quality: REASONABLE

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

DNA repair and recombination protein RAD54-like

Homo sapiens

UniProt Q92698

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 × 12 DNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain A; UniProt 1–10 Chain B; UniProt 1–10 Chain C; UniProt 1–10 Chain D; UniProt 1–10 Chain E; UniProt 1–10 Chain F; UniProt 1–10 Non-standard monomer:Yes (specific site not provided by mmCIF) DNA × 1 DNA repair protein RAD51 homolog 1 × 6 (Q06609) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 CA CALCIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name RAD54_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–11; UniProt 1–10 Author chain B; PDBConstruct 2–11; UniProt 1–10 Author chain C; PDBConstruct 2–11; UniProt 1–10 Author chain D; PDBConstruct 2–11; UniProt 1–10 Author chain E; PDBConstruct 2–11; UniProt 1–10 Author chain F; PDBConstruct 2–11; UniProt 1–10

DNA repair protein RAD51 homolog 1

Homo sapiens

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 × 12 DNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain I; UniProt 1–339 Chain J; UniProt 1–339 Chain K; UniProt 1–339 Chain L; UniProt 1–339 Chain M; UniProt 1–339 Chain N; UniProt 1–339 Not recorded DNA × 1 DNA repair and recombination protein RAD54-like × 6 (Q92698) ATP ADENOSINE-5'-TRIPHOSPHATE × 6 CA CALCIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 3
Chains and sequence ranges Author chain I; PDBConstruct 1–339; UniProt 1–339 Author chain J; PDBConstruct 1–339; UniProt 1–339 Author chain K; PDBConstruct 1–339; UniProt 1–339 Author chain L; PDBConstruct 1–339; UniProt 1–339 Author chain M; PDBConstruct 1–339; UniProt 1–339 Author chain N; PDBConstruct 1–339; UniProt 1–339

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 9tyy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9tyy
Deposition date deposition_date2026-01-21
Structure title titleRAD51-ssDNA filament in complex with calcium and ATP bound by the RAD54 N-terminus
Keywords keywordsRAD51 recombinase, RAD54, 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_guinier43.85
Radius of gyration Rg (electron density) rg_electron43.83
Forward intensity I(0) i0771313000.00
Molecular weight molecular_weight220090.0 kDa
Excluded volume excluded_volume271900 ų
Envelope volume envelope_volume347150 ų
Hydration-shell volume shell_volume64911 ų
Envelope diameter envelope_diameter156.1
Shell Rg shell_rg49.40
Envelope Rg envelope_rg43.70
Shape Rg shape_rg43.84
Total Rg total_rg44.02
Total atoms total_atoms15361
Residues n_residues1944
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 dmax146.9
Rg (real space) rg_real45.56
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real7.6880e+08
I(0) uncertainty (real space) i0_real_error1.1180e+07
Rg (reciprocal space) rg_reciprocal43.85
I(0) (reciprocal space) i0_reciprocal771200000.0000
Solution quality estimate total_estimate0.6801
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.8
Skewness Skewness skewness0.422
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha1.9150
Highest regularization parameter α highest_alpha312500000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 0.890; Sysdev: 0.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.637

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)