7rjn

Crystal structure of human bromodomain containing protein 3 (BRD3) in complex with BCLTF1

Method: X-RAY DIFFRACTION Dmax: 61.0 Å Quality: GOOD

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

Bromodomain-containing protein 3

Homo sapiens

UniProt Q15059

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 24–144 Not recorded Bcl-2-associated transcription factor 1 × 1 (Q9NYF8) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, 30% w/v PEG4000 Resolution 1.95 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 24–144 Not recorded Bcl-2-associated transcription factor 1 × 1 (Q9NYF8) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, 30% w/v PEG4000 Resolution 1.95 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.

47 other PDB entries and 100 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRD3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–123; UniProt 24–144 Author chain B; PDBConstruct 3–123; UniProt 24–144

Bcl-2-associated transcription factor 1

OrganismNot specified

UniProt Q9NYF8

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 C; UniProt 330–339 Fragment:UNP residues 330-339 Non-standard monomer:Yes (specific site not provided by mmCIF) Bromodomain-containing protein 3 × 1 (Q15059) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, 30% w/v PEG4000 Resolution 1.95 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 330–339 Fragment:UNP residues 330-339 Non-standard monomer:Yes (specific site not provided by mmCIF) Bromodomain-containing protein 3 × 1 (Q15059) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate, 30% w/v PEG4000 Resolution 1.95 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCLF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 330–339 Author chain D; PDBConstruct 1–10; UniProt 330–339

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 7rjn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7rjn
Deposition date deposition_date2021-07-21
Structure title titleCrystal structure of human bromodomain containing protein 3 (BRD3) in complex with BCLTF1
Keywords keywordsBRD3, BCL2TF, acetyllysine, 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_guinier19.30
Radius of gyration Rg (electron density) rg_electron18.31
Forward intensity I(0) i014607000.00
Molecular weight molecular_weight29782.0 kDa
Excluded volume excluded_volume37648 ų
Envelope volume envelope_volume42730 ų
Hydration-shell volume shell_volume19299 ų
Envelope diameter envelope_diameter61.5
Shell Rg shell_rg24.74
Envelope Rg envelope_rg18.57
Shape Rg shape_rg18.31
Total Rg total_rg19.23
Total atoms total_atoms2089
Residues n_residues248
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 dmax61.0
Rg (real space) rg_real19.19
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.4610e+07
I(0) uncertainty (real space) i0_real_error1.7930e+05
Rg (reciprocal space) rg_reciprocal19.20
I(0) (reciprocal space) i0_reciprocal14610000.0000
Solution quality estimate total_estimate0.8168
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.160
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6127000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)