9dxg

attP bound large serine integrase and RDF complex in the dimeric state (cleaved)

Method: ELECTRON MICROSCOPY Dmax: 214.4 Å Quality: GOOD

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

Resolvase homolog YokA,SPbeta prophage-derived uncharacterized protein YotN

Bacillus subtilis

UniProt O32006

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–545 Chain B; UniProt 1–545 Chain C; UniProt 1–545 Chain D; UniProt 1–545 Not recorded DNA (34-MER) × 2 DNA (33-MER) × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.61 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YOKA_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–545; UniProt 1–545 Author chain B; PDBConstruct 1–545; UniProt 1–545 Author chain C; PDBConstruct 1–545; UniProt 1–545 Author chain D; PDBConstruct 1–545; UniProt 1–545

Resolvase homolog YokA,SPbeta prophage-derived uncharacterized protein YotN

Bacillus subtilis

UniProt O34850

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 DNA 4 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 2–58 Chain B; UniProt 2–58 Chain C; UniProt 2–58 Chain D; UniProt 2–58 Not recorded DNA (34-MER) × 2 DNA (33-MER) × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.61 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YOTN_BACSU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 564–620; UniProt 2–58 Author chain B; PDBConstruct 564–620; UniProt 2–58 Author chain C; PDBConstruct 564–620; UniProt 2–58 Author chain D; PDBConstruct 564–620; UniProt 2–58

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 9dxg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dxg
Deposition date deposition_date2024-10-11
Structure title titleattP bound large serine integrase and RDF complex in the dimeric state (cleaved)
Keywords keywordsViral protein, Integrase, Recombinase, Complex, Recombination Directionality Factor, Integration, Excision, 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_guinier51.86
Radius of gyration Rg (electron density) rg_electron50.64
Forward intensity I(0) i0618811000.00
Molecular weight molecular_weight179220.0 kDa
Excluded volume excluded_volume213190 ų
Envelope volume envelope_volume307090 ų
Hydration-shell volume shell_volume54942 ų
Envelope diameter envelope_diameter218.0
Shell Rg shell_rg48.36
Envelope Rg envelope_rg50.95
Shape Rg shape_rg50.52
Total Rg total_rg50.92
Total atoms total_atoms23754
Residues n_residues1316
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 dmax214.4
Rg (real space) rg_real52.47
Rg uncertainty (real space) rg_real_error3.58
I(0) (real space) i0_real6.1880e+08
I(0) uncertainty (real space) i0_real_error1.5490e+07
Rg (reciprocal space) rg_reciprocal51.38
I(0) (reciprocal space) i0_reciprocal617900000.0000
Solution quality estimate total_estimate0.7560
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.702
Kurtosis Kurtosis kurtosis0.363
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22160000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.414; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.620; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)