1e6i

Bromodomain from GCN5 complexed with acetylated H4 peptide

Method: X-RAY DIFFRACTION Dmax: 52.3 Å Quality: GOOD

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

TRANSCRIPTIONAL ACTIVATOR GCN5

SACCHAROMYCES CEREVISIAE

UniProt Q03330

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 319–439 Fragment:BROMODOMAIN HISTONE H4 × 1 (P02309) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.2M AMMONIUM SULPHATE, 20% V/V GLYCEROL, 4MM DITHIOTHREITOL, 100 MM HEPES PH 7.5, 125MM NACL 5:1 PEPTIDE:PROTEIN Resolution 1.87 Å R-free 0.209

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN5_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–121; UniProt 319–439

HISTONE H4

OrganismNot specified

UniProt P02309

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 P; UniProt 16–30 Fragment:ACETYLATED TAIL, RESIDUES 16-30 Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSCRIPTIONAL ACTIVATOR GCN5 × 1 (Q03330) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.2M AMMONIUM SULPHATE, 20% V/V GLYCEROL, 4MM DITHIOTHREITOL, 100 MM HEPES PH 7.5, 125MM NACL 5:1 PEPTIDE:PROTEIN Resolution 1.87 Å R-free 0.209

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.

43 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–15; UniProt 16–30

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 1e6i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e6i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e6i
Deposition date deposition_date2000-08-18
Structure title titleBromodomain from GCN5 complexed with acetylated H4 peptide
Keywords keywordsGENE REGULATION, HISTONE BINDING, N-ACETYL LYSINE; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.74
Radius of gyration Rg (electron density) rg_electron14.45
Forward intensity I(0) i03880810.00
Molecular weight molecular_weight13896.0 kDa
Excluded volume excluded_volume17345 ų
Envelope volume envelope_volume19884 ų
Hydration-shell volume shell_volume11896 ų
Envelope diameter envelope_diameter51.3
Shell Rg shell_rg19.97
Envelope Rg envelope_rg14.88
Shape Rg shape_rg14.45
Total Rg total_rg15.60
Total atoms total_atoms981
Residues n_residues116
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 dmax52.3
Rg (real space) rg_real15.70
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real3.8810e+06
I(0) uncertainty (real space) i0_real_error4.2180e+04
Rg (reciprocal space) rg_reciprocal15.71
I(0) (reciprocal space) i0_reciprocal3881000.0000
Solution quality estimate total_estimate0.8791
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.291
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha884400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1e6ia_
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.2 — Bromodomain
Family Family familya.29.2.1 — Bromodomain

CATH v4.4 (1 domains)

Domain ID domain_id1e6iA00
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)