3muk

Crystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23

Method: X-RAY DIFFRACTION Dmax: 58.3 Å Quality: GOOD

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

Bromodomain-containing protein 4

Mus musculus

UniProt Q9ESU6

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 42–168 Fragment:bromodomain, UNP residues 42-168 peptide of Histone H3.3 × 1 (P84243) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;3.6M Na formate, 10% glycerol, soaked with 20-times excess of histone octapeptide, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.219

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRD4_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–131; UniProt 42–168

peptide of Histone H3.3

OrganismNot specified

UniProt P84243

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 22–29 Fragment:histone H3 peptide, UNP residues 22-29 Non-standard monomer:Yes (specific site not provided by mmCIF) Bromodomain-containing protein 4 × 1 (Q9ESU6) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;3.6M Na formate, 10% glycerol, soaked with 20-times excess of histone octapeptide, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.75 Å R-free 0.219

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.

94 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–8; UniProt 22–29

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 3muk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3muk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3muk
Deposition date deposition_date2010-05-03
Structure title titleCrystal structure of Brd4 bromodomain 1 with propionylated histone H3-K(prop)23
Keywords keywordsbromodomain, histone recognition, N-propionyl lysine, acylation, 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_guinier16.37
Radius of gyration Rg (electron density) rg_electron15.24
Forward intensity I(0) i04171840.00
Molecular weight molecular_weight15178.0 kDa
Excluded volume excluded_volume19240 ų
Envelope volume envelope_volume21707 ų
Hydration-shell volume shell_volume12403 ų
Envelope diameter envelope_diameter56.8
Shell Rg shell_rg20.65
Envelope Rg envelope_rg15.74
Shape Rg shape_rg15.24
Total Rg total_rg16.31
Total atoms total_atoms1071
Residues n_residues133
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 dmax58.3
Rg (real space) rg_real16.36
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.1720e+06
I(0) uncertainty (real space) i0_real_error5.5220e+04
Rg (reciprocal space) rg_reciprocal16.36
I(0) (reciprocal space) i0_reciprocal4172000.0000
Solution quality estimate total_estimate0.8505
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.8
Skewness Skewness skewness0.343
Kurtosis Kurtosis kurtosis-0.238
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha976400.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3mukA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like

8. Citations (1)

9. Files and Curves (10)