9qn8

RAD51 filament in complex with calcium and ATP bound by the RAD51AP1 C-terminus

Method: ELECTRON MICROSCOPY Dmax: 150.1 Å Quality: REASONABLE

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 Heteromer Protein × 12 DNA 1 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain A; UniProt 1–339 Chain C; UniProt 1–339 Chain E; UniProt 1–339 Chain G; UniProt 1–339 Chain I; UniProt 1–339 Chain K; UniProt 1–339 Not recorded RAD51-associated protein 1 × 6 (Q96B01) DNA × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 7 K POTASSIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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 C; PDBConstruct 1–339; UniProt 1–339 Author chain E; PDBConstruct 1–339; UniProt 1–339 Author chain G; PDBConstruct 1–339; UniProt 1–339 Author chain I; PDBConstruct 1–339; UniProt 1–339 Author chain K; PDBConstruct 1–339; UniProt 1–339

RAD51-associated protein 1

Homo sapiens

UniProt Q96B01

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 B; UniProt 1–352 Chain D; UniProt 1–352 Chain F; UniProt 1–352 Chain H; UniProt 1–352 Chain J; UniProt 1–352 Chain L; UniProt 1–352 Not recorded DNA repair protein RAD51 homolog 1 × 6 (Q06609) DNA × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 7 CA CALCIUM ION × 7 K POTASSIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.14 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name R51A1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–354; UniProt 1–352 Author chain D; PDBConstruct 3–354; UniProt 1–352 Author chain F; PDBConstruct 3–354; UniProt 1–352 Author chain H; PDBConstruct 3–354; UniProt 1–352 Author chain J; PDBConstruct 3–354; UniProt 1–352 Author chain L; PDBConstruct 3–354; UniProt 1–352

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 9qn8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qn8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qn8
Deposition date deposition_date2025-03-24
Structure title titleRAD51 filament in complex with calcium and ATP bound by the RAD51AP1 C-terminus
Keywords keywordsRAD51 recombinase, RAD51AP1, filament modulation, homologous recombination, nucleotide hydrolysis, 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_guinier45.18
Radius of gyration Rg (electron density) rg_electron45.14
Forward intensity I(0) i0822988000.00
Molecular weight molecular_weight228510.0 kDa
Excluded volume excluded_volume282710 ų
Envelope volume envelope_volume386690 ų
Hydration-shell volume shell_volume70454 ų
Envelope diameter envelope_diameter161.8
Shell Rg shell_rg50.34
Envelope Rg envelope_rg44.82
Shape Rg shape_rg45.15
Total Rg total_rg45.30
Total atoms total_atoms15950
Residues n_residues2025
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 dmax150.1
Rg (real space) rg_real45.26
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real8.2300e+08
I(0) uncertainty (real space) i0_real_error1.4860e+07
Rg (reciprocal space) rg_reciprocal45.18
I(0) (reciprocal space) i0_reciprocal822900000.0000
Solution quality estimate total_estimate0.6401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha399200000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 0.010; Positv: 1.000; Valcen: 0.950; Smooth: 0.737

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)