8pbd

RAD51 filament on dsDNA bound by the BRCA2 c-terminus

Method: ELECTRON MICROSCOPY Dmax: 199.6 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 Heteromer Protein × 19 DNA 2 PDB declaration: 21-meric(21) 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 Chain J; UniProt 1–339 Not recorded Breast cancer type 2 susceptibility protein × 9 (P51587) DNA strand 1 × 1 DNA strand 2 × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 10 CA CALCIUM ION × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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 Author chain J; PDBConstruct 1–339; UniProt 1–339

Breast cancer type 2 susceptibility protein

OrganismNot specified

UniProt P51587

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 × 19 DNA 2 PDB declaration: 21-meric(21) Consistent with all polymer counts Chain K; UniProt 3260–3308 Chain L; UniProt 3260–3308 Chain M; UniProt 3260–3308 Chain N; UniProt 3260–3308 Chain O; UniProt 3260–3308 Chain P; UniProt 3260–3308 Chain Q; UniProt 3260–3308 Chain R; UniProt 3260–3308 Chain S; UniProt 3260–3308 Not recorded DNA repair protein RAD51 homolog 1 × 10 (Q06609) DNA strand 1 × 1 DNA strand 2 × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 10 CA CALCIUM ION × 20 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.83 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.

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

View Construct and Data Evidence
UniProt name BRCA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–49; UniProt 3260–3308 Author chain L; PDBConstruct 1–49; UniProt 3260–3308 Author chain M; PDBConstruct 1–49; UniProt 3260–3308 Author chain N; PDBConstruct 1–49; UniProt 3260–3308 Author chain O; PDBConstruct 1–49; UniProt 3260–3308 Author chain P; PDBConstruct 1–49; UniProt 3260–3308 Author chain Q; PDBConstruct 1–49; UniProt 3260–3308 Author chain R; PDBConstruct 1–49; UniProt 3260–3308 Author chain S; PDBConstruct 1–49; UniProt 3260–3308

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 8pbd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pbd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pbd
Deposition date deposition_date2023-06-09
最后修订 last_revision2023-11-15
Structure title titleRAD51 filament on dsDNA bound by the BRCA2 c-terminus
Keywords keywordsRAD51, BRCA2, Filament, Complex, RECOMBINATION; RECOMBINATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.88
Radius of gyration Rg (electron density) rg_electron56.32
Forward intensity I(0) i02253790000.00
Molecular weight molecular_weight377950.0 kDa
Excluded volume excluded_volume465100 ų
Envelope volume envelope_volume652060 ų
Hydration-shell volume shell_volume96623 ų
Envelope diameter envelope_diameter220.4
Shell Rg shell_rg58.93
Envelope Rg envelope_rg55.50
Shape Rg shape_rg56.34
Total Rg total_rg56.34
Total atoms total_atoms26366
Residues n_residues3308
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 dmax199.6
Rg (real space) rg_real56.10
Rg uncertainty (real space) rg_real_error2.29
I(0) (real space) i0_real2.2540e+09
I(0) uncertainty (real space) i0_real_error5.0250e+07
Rg (reciprocal space) rg_reciprocal55.69
I(0) (reciprocal space) i0_reciprocal2252000000.0000
Solution quality estimate total_estimate0.8402
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.3
Skewness Skewness skewness0.448
Kurtosis Kurtosis kurtosis-0.132
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha759200000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.748

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)