8tfu

Structure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 1

Method: X-RAY DIFFRACTION Dmax: 61.3 Å Quality: GOOD

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

Recombination protein bet

Escherichia phage Lambda

UniProt P03698

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 182–261 Mutation:GSHM Plasmid-derived single-stranded DNA-binding protein × 1 (P28044) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;293 K;0.48 M sodium phosphate monobasic monohydrate, 1.2 M potassium phosphate dibasic Resolution 1.48 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 182–261 Mutation:GSHM Plasmid-derived single-stranded DNA-binding protein × 1 (P28044) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;293 K;0.48 M sodium phosphate monobasic monohydrate, 1.2 M potassium phosphate dibasic Resolution 1.48 Å R-free 0.220

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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VBET_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–84; UniProt 182–261 Author chain B; PDBConstruct 5–84; UniProt 182–261

Plasmid-derived single-stranded DNA-binding protein

OrganismNot specified

UniProt P28044

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 166–175 Fragment:C-terminal peptide Recombination protein bet × 1 (P03698) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;293 K;0.48 M sodium phosphate monobasic monohydrate, 1.2 M potassium phosphate dibasic Resolution 1.48 Å R-free 0.220
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 166–175 Fragment:C-terminal peptide Recombination protein bet × 1 (P03698) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;293 K;0.48 M sodium phosphate monobasic monohydrate, 1.2 M potassium phosphate dibasic Resolution 1.48 Å R-free 0.220

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SSB7_ECOLX
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 166–175 Author chain D; PDBConstruct 1–10; UniProt 166–175

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 8tfu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8tfu
Deposition date deposition_date2023-07-11
Structure title titleStructure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 1
Keywords keywords;Recombination, Recombineering, Single Strand Annealing, Single-stranded DNA binding protein, genome engineering, 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_guinier18.32
Radius of gyration Rg (electron density) rg_electron17.33
Forward intensity I(0) i06049370.00
Molecular weight molecular_weight17894.0 kDa
Excluded volume excluded_volume22394 ų
Envelope volume envelope_volume27279 ų
Hydration-shell volume shell_volume13929 ų
Envelope diameter envelope_diameter59.8
Shell Rg shell_rg22.37
Envelope Rg envelope_rg17.51
Shape Rg shape_rg17.31
Total Rg total_rg18.29
Total atoms total_atoms1258
Residues n_residues159
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 dmax61.3
Rg (real space) rg_real18.32
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real6.0490e+06
I(0) uncertainty (real space) i0_real_error7.9290e+04
Rg (reciprocal space) rg_reciprocal18.32
I(0) (reciprocal space) i0_reciprocal6049000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1460000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; 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 (3)

8. Citations (1)

9. Files and Curves (10)