9svx

XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on single stranded DNA

Method: ELECTRON MICROSCOPY Dmax: 187.3 Å Quality: GOOD

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

DNA repair protein RAD51 homolog 3

Homo sapiens

UniProt O43502

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 × 9 DNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain C; UniProt 1–376 Not recorded ssDNA × 1 DNA repair protein XRCC3 × 1 (O43542) DNA repair protein RAD51 homolog 4 × 1 (O75771) DNA repair protein XRCC2 × 1 (O43543) DNA repair protein RAD51 homolog 1 × 5 (Q06609) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RA51C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–376; UniProt 1–376

DNA repair protein XRCC3

Homo sapiens

UniProt O43542

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 × 9 DNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain D; UniProt 1–346 Not recorded ssDNA × 1 DNA repair protein RAD51 homolog 3 × 1 (O43502) DNA repair protein RAD51 homolog 4 × 1 (O75771) DNA repair protein XRCC2 × 1 (O43543) DNA repair protein RAD51 homolog 1 × 5 (Q06609) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XRCC3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–346; UniProt 1–346

DNA repair protein RAD51 homolog 4

Homo sapiens

UniProt O75771

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 × 9 DNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain B; UniProt 1–328 Not recorded ssDNA × 1 DNA repair protein RAD51 homolog 3 × 1 (O43502) DNA repair protein XRCC3 × 1 (O43542) DNA repair protein XRCC2 × 1 (O43543) DNA repair protein RAD51 homolog 1 × 5 (Q06609) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RA51D_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–328; UniProt 1–328

DNA repair protein XRCC2

Homo sapiens

UniProt O43543

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 × 9 DNA 1 PDB declaration: decameric(10) Consistent with all polymer counts Chain A; UniProt 1–280 Not recorded ssDNA × 1 DNA repair protein RAD51 homolog 3 × 1 (O43502) DNA repair protein XRCC3 × 1 (O43542) DNA repair protein RAD51 homolog 4 × 1 (O75771) DNA repair protein RAD51 homolog 1 × 5 (Q06609) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name XRCC2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–280; UniProt 1–280

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 × 9 DNA 1 PDB declaration: decameric(10) Consistent with all polymer counts 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 ssDNA × 1 DNA repair protein RAD51 homolog 3 × 1 (O43502) DNA repair protein XRCC3 × 1 (O43542) DNA repair protein RAD51 homolog 4 × 1 (O75771) DNA repair protein XRCC2 × 1 (O43543) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 6
Chains and sequence ranges 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 9svx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9svx
Deposition date deposition_date2025-10-03
Structure title titleXRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on single stranded DNA
Keywords keywordsDNA binding protein, complex, tumor suppresor; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.34
Radius of gyration Rg (electron density) rg_electron54.61
Forward intensity I(0) i01486370000.00
Molecular weight molecular_weight313730.0 kDa
Excluded volume excluded_volume389500 ų
Envelope volume envelope_volume560560 ų
Hydration-shell volume shell_volume85498 ų
Envelope diameter envelope_diameter201.9
Shell Rg shell_rg57.77
Envelope Rg envelope_rg53.61
Shape Rg shape_rg54.63
Total Rg total_rg54.65
Total atoms total_atoms21935
Residues n_residues2782
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 dmax187.3
Rg (real space) rg_real54.44
Rg uncertainty (real space) rg_real_error2.14
I(0) (real space) i0_real1.4860e+09
I(0) uncertainty (real space) i0_real_error2.9450e+07
Rg (reciprocal space) rg_reciprocal54.24
I(0) (reciprocal space) i0_reciprocal1486000000.0000
Solution quality estimate total_estimate0.8588
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.0
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha277900000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.707

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)