7t7t

Structure of TSK/BRU1 bound to histone H3.1

Method: X-RAY DIFFRACTION Dmax: 135.9 Å Quality: GOOD

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

Protein TONSOKU

Citrus unshiu

UniProt A0A2H5Q1B8

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 1–490 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.1 × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;294.15 K;25% 1,2-Propanediol, 20% glycerol, 0.1M sodium potassium phosphate pH 6 Resolution 3.17 Å R-free 0.318
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–490 Non-standard monomer:Yes (specific site not provided by mmCIF) Histone H3.1 × 1 (P59226) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;294.15 K;25% 1,2-Propanediol, 20% glycerol, 0.1M sodium potassium phosphate pH 6 Resolution 3.17 Å R-free 0.318

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A2H5Q1B8_CITUN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 42–531; UniProt 1–490 Author chain B; PDBConstruct 42–531; UniProt 1–490

Histone H3.1

OrganismNot specified

UniProt P59226

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 W; UniProt 2–46 Not recorded Protein TONSOKU × 1 (A0A2H5Q1B8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;294.15 K;25% 1,2-Propanediol, 20% glycerol, 0.1M sodium potassium phosphate pH 6 Resolution 3.17 Å R-free 0.318
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain X; UniProt 2–46 Not recorded Protein TONSOKU × 1 (A0A2H5Q1B8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;294.15 K;25% 1,2-Propanediol, 20% glycerol, 0.1M sodium potassium phosphate pH 6 Resolution 3.17 Å R-free 0.318

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.

36 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H32_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain W; PDBConstruct 1–45; UniProt 2–46 Author chain X; PDBConstruct 1–45; UniProt 2–46

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 7t7t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7t7t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7t7t
Deposition date deposition_date2021-12-15
Structure title titleStructure of TSK/BRU1 bound to histone H3.1
Keywords keywordsEpigenetic protein, H3.1 reader, nucleosome, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.13
Radius of gyration Rg (electron density) rg_electron37.16
Forward intensity I(0) i0184753000.00
Molecular weight molecular_weight103690.0 kDa
Excluded volume excluded_volume126840 ų
Envelope volume envelope_volume174560 ų
Hydration-shell volume shell_volume41026 ų
Envelope diameter envelope_diameter148.1
Shell Rg shell_rg41.09
Envelope Rg envelope_rg36.65
Shape Rg shape_rg37.16
Total Rg total_rg37.44
Total atoms total_atoms7175
Residues n_residues918
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 dmax135.9
Rg (real space) rg_real37.39
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real1.8480e+08
I(0) uncertainty (real space) i0_real_error3.4530e+06
Rg (reciprocal space) rg_reciprocal37.23
I(0) (reciprocal space) i0_reciprocal184700000.0000
Solution quality estimate total_estimate0.8325
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis-0.127
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16260000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.705; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)