9om8

Crystal structure of PprA S-F filament from Deinococcus radiodurans

Method: X-RAY DIFFRACTION Dmax: 113.2 Å Quality: EXCELLENT

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

DNA repair protein PprA

Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539

UniProt O32504

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 homooligomer Homooligomer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 25–300 Chain B; UniProt 25–300 Chain C; UniProt 25–300 Chain D; UniProt 25–300 Mutation:D180K, D184K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;1.0 ul of protein solution was mixed with 1.0 uL of crystallization solution and hung upside-down in a sealed chamber containing 1mL of well solution. | Protein solution: 3.5 mg/mL PprA (117 uM), 150mM KCl, 20mM Tris, pH 7.5 | Crystallization solution: 0.2M LiCl, 20% (w/v) PEG 3350 | Well solution: 1.4 M (NH4)2SO4 Resolution 2.83 Å R-free 0.275

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPRA_DEIRA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–277; UniProt 25–300 Author chain B; PDBConstruct 2–277; UniProt 25–300 Author chain C; PDBConstruct 2–277; UniProt 25–300 Author chain D; PDBConstruct 2–277; UniProt 25–300

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 9om8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9om8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9om8
Deposition date deposition_date2025-05-13
最后修订 last_revision2025-05-28
Structure title titleCrystal structure of PprA S-F filament from Deinococcus radiodurans
Keywords keywords;PprA, Deinococcus, Deinococcus radiodurans, D. radiodurans, DNA repair, DNA binding protein, Genome reassembly, self-assembly, protein filament ;; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.10
Radius of gyration Rg (electron density) rg_electron34.52
Forward intensity I(0) i0186053000.00
Molecular weight molecular_weight105450.0 kDa
Excluded volume excluded_volume130450 ų
Envelope volume envelope_volume184920 ų
Hydration-shell volume shell_volume44994 ų
Envelope diameter envelope_diameter121.6
Shell Rg shell_rg40.90
Envelope Rg envelope_rg34.03
Shape Rg shape_rg34.52
Total Rg total_rg35.01
Total atoms total_atoms7449
Residues n_residues1003
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 dmax113.2
Rg (real space) rg_real35.05
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real1.8610e+08
I(0) uncertainty (real space) i0_real_error2.8490e+06
Rg (reciprocal space) rg_reciprocal35.08
I(0) (reciprocal space) i0_reciprocal186100000.0000
Solution quality estimate total_estimate0.9020
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.3
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23650000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)