8tg8

Structure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 3

Method: X-RAY DIFFRACTION Dmax: 41.9 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 TRP-MET-ASP-PHE-ASP-ASP-ASP-ILE-PRO-PHE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.6;298 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M Tris pH 8.6 Resolution 1.58 Å R-free 0.232

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 9 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

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 8tg8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tg8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tg8
Deposition date deposition_date2023-07-12
Structure title titleStructure of Red beta C-terminal domain in complex with SSB C-terminal peptide, Form 3
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_guinier13.36
Radius of gyration Rg (electron density) rg_electron11.77
Forward intensity I(0) i01631170.00
Molecular weight molecular_weight8646.0 kDa
Excluded volume excluded_volume10848 ų
Envelope volume envelope_volume12261 ų
Hydration-shell volume shell_volume9078 ų
Envelope diameter envelope_diameter40.5
Shell Rg shell_rg17.16
Envelope Rg envelope_rg12.15
Shape Rg shape_rg11.77
Total Rg total_rg13.16
Total atoms total_atoms608
Residues n_residues77
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 dmax41.9
Rg (real space) rg_real13.27
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.6310e+06
I(0) uncertainty (real space) i0_real_error1.7290e+04
Rg (reciprocal space) rg_reciprocal13.28
I(0) (reciprocal space) i0_reciprocal1631000.0000
Solution quality estimate total_estimate0.8071
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.063
Kurtosis Kurtosis kurtosis-0.353
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha256400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; 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)