9i62

CryoEM structure of a RAD51 D-loop

Method: ELECTRON MICROSCOPY Dmax: 189.9 Å Quality: GOOD

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

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 Homooligomer Protein × 9 DNA 3 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 Chain G; UniProt 1–339 Chain H; UniProt 1–339 Chain I; UniProt 1–339 Not recorded DNA (26-MER) × 1 DNA (41-MER) × 1 DNA (41-MER) × 1 CA CALCIUM ION × 18 ATP ADENOSINE-5'-TRIPHOSPHATE × 9 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.64 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 Author chain G; PDBConstruct 1–339; UniProt 1–339 Author chain H; PDBConstruct 1–339; UniProt 1–339 Author chain I; 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 9i62

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i62
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i62
Deposition date deposition_date2025-01-29
Structure title titleCryoEM structure of a RAD51 D-loop
Keywords keywordsDNA REPAIR, HOMOLOGOUS RECOMBINATION, STRAND EXCHANGE, ATPASE, 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_guinier51.54
Radius of gyration Rg (electron density) rg_electron52.04
Forward intensity I(0) i02042380000.00
Molecular weight molecular_weight347470.0 kDa
Excluded volume excluded_volume422560 ų
Envelope volume envelope_volume584130 ų
Hydration-shell volume shell_volume92608 ų
Envelope diameter envelope_diameter200.3
Shell Rg shell_rg56.10
Envelope Rg envelope_rg51.76
Shape Rg shape_rg52.06
Total Rg total_rg52.06
Total atoms total_atoms24161
Residues n_residues2939
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 dmax189.9
Rg (real space) rg_real51.62
Rg uncertainty (real space) rg_real_error2.32
I(0) (real space) i0_real2.0420e+09
I(0) uncertainty (real space) i0_real_error4.7940e+07
Rg (reciprocal space) rg_reciprocal51.47
I(0) (reciprocal space) i0_reciprocal2042000000.0000
Solution quality estimate total_estimate0.8472
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.2
Skewness Skewness skewness0.416
Kurtosis Kurtosis kurtosis-0.175
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha392900000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.712; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)