9j1s

Human replication protein A: RPA70 subunit N-terminal domain

Method: X-RAY DIFFRACTION Dmax: 45.6 Å Quality: GOOD

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

Replication protein A 70 kDa DNA-binding subunit

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–120 Fragment:N-terminal domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;0.2 M Ammonium sulfate, 0.1 M Bis-Tris, pH 7.0, 25% PEG 3350 Resolution 1.55 Å R-free 0.230

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 1–120; UniProt 1–120

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 9j1s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j1s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j1s
Deposition date deposition_date2024-08-05
最后修订 last_revision2024-10-09
Structure title titleHuman replication protein A: RPA70 subunit N-terminal domain
Keywords keywordsReplication, Single strand binding, DNA binding, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.64
Radius of gyration Rg (electron density) rg_electron13.07
Forward intensity I(0) i03017410.00
Molecular weight molecular_weight12186.0 kDa
Excluded volume excluded_volume15358 ų
Envelope volume envelope_volume17141 ų
Hydration-shell volume shell_volume11191 ų
Envelope diameter envelope_diameter44.6
Shell Rg shell_rg18.80
Envelope Rg envelope_rg13.42
Shape Rg shape_rg13.10
Total Rg total_rg14.29
Total atoms total_atoms853
Residues n_residues114
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 dmax45.6
Rg (real space) rg_real14.53
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real3.0170e+06
I(0) uncertainty (real space) i0_real_error3.2470e+04
Rg (reciprocal space) rg_reciprocal14.54
I(0) (reciprocal space) i0_reciprocal3017000.0000
Solution quality estimate total_estimate0.8931
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.098
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha499200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)