8rk2

Human Replication protein A (RPA; trimeric core) - ssDNA complex

Method: ELECTRON MICROSCOPY Dmax: 91.0 Å Quality: REASONABLE

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

Replication protein A 70 kDa DNA-binding subunit, N-terminally processed

Homo sapiens

UniProt P27694

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–616 Not recorded Replication protein A 32 kDa subunit × 1 (P15927) Replication protein A 14 kDa subunit × 1 (P35244) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–616; UniProt 1–616

Replication protein A 32 kDa subunit

Homo sapiens

UniProt P15927

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–270 Not recorded Replication protein A 70 kDa DNA-binding subunit, N-terminally processed × 1 (P27694) Replication protein A 14 kDa subunit × 1 (P35244) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

13 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–270; UniProt 1–270

Replication protein A 14 kDa subunit

Homo sapiens

UniProt P35244

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–121 Not recorded Replication protein A 70 kDa DNA-binding subunit, N-terminally processed × 1 (P27694) Replication protein A 32 kDa subunit × 1 (P15927) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 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.

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–121; UniProt 1–121

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 8rk2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rk2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rk2
Deposition date deposition_date2023-12-22
Structure title titleHuman Replication protein A (RPA; trimeric core) - ssDNA complex
Keywords keywordsssDNA binding protein, DNA damage repair, Single-strand annealing, 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_guinier26.76
Radius of gyration Rg (electron density) rg_electron25.89
Forward intensity I(0) i035641900.00
Molecular weight molecular_weight46242.0 kDa
Excluded volume excluded_volume58075 ų
Envelope volume envelope_volume76697 ų
Hydration-shell volume shell_volume26076 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg31.47
Envelope Rg envelope_rg25.98
Shape Rg shape_rg25.84
Total Rg total_rg26.71
Total atoms total_atoms6484
Residues n_residues404
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 dmax91.0
Rg (real space) rg_real26.87
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real3.5640e+07
I(0) uncertainty (real space) i0_real_error5.6220e+05
Rg (reciprocal space) rg_reciprocal26.84
I(0) (reciprocal space) i0_reciprocal35640000.0000
Solution quality estimate total_estimate0.6499
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.501
Kurtosis Kurtosis kurtosis-0.095
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5631000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 0.089; Positv: 1.000; Valcen: 0.917; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)