8u4u

Crystal structure of 53BP1 tandem Tudor domain homodimer engineered with two disulfide bridges

Method: X-RAY DIFFRACTION Dmax: 138.4 Å Quality: GOOD

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

TP53-binding protein 1

Homo sapiens

UniProt Q12888

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1484–1603 Chain B; UniProt 1484–1603 Mutation:E1549C, E1567C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Crystals of the protein (15 mg/mL) were obtained by the hanging drop vapor diffusion method, mixing 1 microliter of the sample in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl and 1 microliter of the reservoir solution (0.1 M Bis-Tris, pH 6.5) at 293 K. The crystals were cryoprotected with 25% (w/v) xylitol Resolution 3.79 Å R-free 0.300
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1484–1603 Chain D; UniProt 1484–1603 Mutation:E1549C, E1567C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Crystals of the protein (15 mg/mL) were obtained by the hanging drop vapor diffusion method, mixing 1 microliter of the sample in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl and 1 microliter of the reservoir solution (0.1 M Bis-Tris, pH 6.5) at 293 K. The crystals were cryoprotected with 25% (w/v) xylitol Resolution 3.79 Å R-free 0.300
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1484–1603 Chain F; UniProt 1484–1603 Mutation:E1549C, E1567C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Crystals of the protein (15 mg/mL) were obtained by the hanging drop vapor diffusion method, mixing 1 microliter of the sample in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl and 1 microliter of the reservoir solution (0.1 M Bis-Tris, pH 6.5) at 293 K. The crystals were cryoprotected with 25% (w/v) xylitol Resolution 3.79 Å R-free 0.300
4 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1484–1603 Chain H; UniProt 1484–1603 Mutation:E1549C, E1567C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Crystals of the protein (15 mg/mL) were obtained by the hanging drop vapor diffusion method, mixing 1 microliter of the sample in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl and 1 microliter of the reservoir solution (0.1 M Bis-Tris, pH 6.5) at 293 K. The crystals were cryoprotected with 25% (w/v) xylitol Resolution 3.79 Å R-free 0.300
5 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1484–1603 Chain J; UniProt 1484–1603 Mutation:E1549C, E1567C No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;Crystals of the protein (15 mg/mL) were obtained by the hanging drop vapor diffusion method, mixing 1 microliter of the sample in 50 mM Tris-HCl, pH 7.0, 100 mM NaCl and 1 microliter of the reservoir solution (0.1 M Bis-Tris, pH 6.5) at 293 K. The crystals were cryoprotected with 25% (w/v) xylitol Resolution 3.79 Å R-free 0.300

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.

34 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TP53B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–125; UniProt 1484–1603 Author chain B; PDBConstruct 6–125; UniProt 1484–1603 Author chain C; PDBConstruct 6–125; UniProt 1484–1603 Author chain D; PDBConstruct 6–125; UniProt 1484–1603 Author chain E; PDBConstruct 6–125; UniProt 1484–1603 Author chain F; PDBConstruct 6–125; UniProt 1484–1603 Author chain G; PDBConstruct 6–125; UniProt 1484–1603 Author chain H; PDBConstruct 6–125; UniProt 1484–1603 Author chain I; PDBConstruct 6–125; UniProt 1484–1603 Author chain J; PDBConstruct 6–125; UniProt 1484–1603

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 8u4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u4u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u4u
Deposition date deposition_date2023-09-11
Structure title titleCrystal structure of 53BP1 tandem Tudor domain homodimer engineered with two disulfide bridges
Keywords keywords;53BP1, DNA damage response, DNA double-strand break repair, non-homologous end joining, homologous recombination, chromatin-binding protein, engineered protein, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.23
Radius of gyration Rg (electron density) rg_electron41.99
Forward intensity I(0) i0265738000.00
Molecular weight molecular_weight134750.0 kDa
Excluded volume excluded_volume169340 ų
Envelope volume envelope_volume239660 ų
Hydration-shell volume shell_volume49276 ų
Envelope diameter envelope_diameter140.5
Shell Rg shell_rg45.36
Envelope Rg envelope_rg40.93
Shape Rg shape_rg41.98
Total Rg total_rg42.21
Total atoms total_atoms18847
Residues n_residues1193
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 dmax138.4
Rg (real space) rg_real42.18
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real2.6570e+08
I(0) uncertainty (real space) i0_real_error4.4950e+06
Rg (reciprocal space) rg_reciprocal42.23
I(0) (reciprocal space) i0_reciprocal265800000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.9
Skewness Skewness skewness0.158
Kurtosis Kurtosis kurtosis-0.639
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34950000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.911

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)