9y6v

attPsym bound large serine integrase and RDF complex in the dimeric state

Method: ELECTRON MICROSCOPY Dmax: 178.7 Å Quality: GOOD

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

Resolvase homolog YokA,SPbeta prophage-derived uncharacterized protein YotN

Spbetavirus SPbeta

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 2 PDB declaration: hexameric(6) 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 attPsym × 1 attPsym × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 100mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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

Spbetavirus SPbeta

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 2 PDB declaration: hexameric(6) 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 attPsym × 1 attPsym × 1 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20mM Tris-HCl, 100mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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 9y6v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y6v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y6v
Deposition date deposition_date2025-09-09
Structure title titleattPsym bound large serine integrase and RDF complex in the dimeric state
Keywords keywords;Site-specific DNA Recombinase, Large serine integrase, DNA binding domains, Recombinase, Resolvase, Zinc ribbon recombinase, RECOMBINATION ;; RECOMBINATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.07
Radius of gyration Rg (electron density) rg_electron46.76
Forward intensity I(0) i0566603000.00
Molecular weight molecular_weight173030.0 kDa
Excluded volume excluded_volume207110 ų
Envelope volume envelope_volume315110 ų
Hydration-shell volume shell_volume59091 ų
Envelope diameter envelope_diameter181.1
Shell Rg shell_rg47.60
Envelope Rg envelope_rg46.10
Shape Rg shape_rg46.69
Total Rg total_rg46.97
Total atoms total_atoms23114
Residues n_residues1296
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 dmax178.7
Rg (real space) rg_real47.48
Rg uncertainty (real space) rg_real_error2.51
I(0) (real space) i0_real5.6660e+08
I(0) uncertainty (real space) i0_real_error1.1080e+07
Rg (reciprocal space) rg_reciprocal47.07
I(0) (reciprocal space) i0_reciprocal566300000.0000
Solution quality estimate total_estimate0.8220
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.1
Skewness Skewness skewness0.536
Kurtosis Kurtosis kurtosis0.031
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33070000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.652; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.842; Smooth: 0.883

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)