8tg7

Structure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 2

Method: X-RAY DIFFRACTION Dmax: 60.8 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:N-terminal GSHM Plasmid-derived single-stranded DNA-binding protein × 1 (P28044) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.6;298 K;2.0 M ammonium sulfate, 0.1 M Tris pH 8.6 Resolution 1.77 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 182–261 Mutation:N-terminal GSHM Plasmid-derived single-stranded DNA-binding protein × 1 (P28044) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.6;298 K;2.0 M ammonium sulfate, 0.1 M Tris pH 8.6 Resolution 1.77 Å R-free 0.234

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 Not recorded Recombination protein bet × 1 (P03698) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.6;298 K;2.0 M ammonium sulfate, 0.1 M Tris pH 8.6 Resolution 1.77 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 166–175 Not recorded Recombination protein bet × 1 (P03698) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.6;298 K;2.0 M ammonium sulfate, 0.1 M Tris pH 8.6 Resolution 1.77 Å R-free 0.234

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 8tg7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tg7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tg7
Deposition date deposition_date2023-07-12
Structure title titleStructure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 2
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_guinier18.08
Radius of gyration Rg (electron density) rg_electron17.16
Forward intensity I(0) i05730380.00
Molecular weight molecular_weight17413.0 kDa
Excluded volume excluded_volume21777 ų
Envelope volume envelope_volume26145 ų
Hydration-shell volume shell_volume13535 ų
Envelope diameter envelope_diameter60.8
Shell Rg shell_rg22.08
Envelope Rg envelope_rg17.38
Shape Rg shape_rg17.14
Total Rg total_rg18.09
Total atoms total_atoms1224
Residues n_residues152
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 dmax60.8
Rg (real space) rg_real18.11
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real5.7300e+06
I(0) uncertainty (real space) i0_real_error7.3250e+04
Rg (reciprocal space) rg_reciprocal18.11
I(0) (reciprocal space) i0_reciprocal5730000.0000
Solution quality estimate total_estimate0.7869
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.376
Kurtosis Kurtosis kurtosis-0.354
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1457000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 0.994; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)