4yym

Crystal structure of TAF1 BD2 Bromodomain bound to a butyryllysine peptide

Method: X-RAY DIFFRACTION Dmax: 92.8 Å Quality: REASONABLE

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

Transcription initiation factor TFIID subunit 1

Homo sapiens

UniProt P21675

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1497–1638 Chain B; UniProt 1497–1638 Fragment:bromodomain (UNP residues 1497-1638) Histone H4 × 1 (P62805) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M calcium chloride, 20 w/v PEG3350 Resolution 1.50 Å R-free 0.261

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.

62 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–144; UniProt 1497–1638 Author chain B; PDBConstruct 3–144; UniProt 1497–1638

Histone H4

OrganismNot specified

UniProt P62805

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain Z; UniProt 2–12 Fragment:N-terminal tail (UNP residues 2-12) Non-standard monomer:Yes (specific site not provided by mmCIF) Transcription initiation factor TFIID subunit 1 × 2 (P21675) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;0.2 M calcium chloride, 20 w/v PEG3350 Resolution 1.50 Å R-free 0.261

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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Z; PDBConstruct 1–11; UniProt 2–12

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 4yym

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yym
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yym
Deposition date deposition_date2015-03-24
Structure title titleCrystal structure of TAF1 BD2 Bromodomain bound to a butyryllysine peptide
Keywords keywordsBromodomain-butyryllysine complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.96
Radius of gyration Rg (electron density) rg_electron24.20
Forward intensity I(0) i016799400.00
Molecular weight molecular_weight31490.0 kDa
Excluded volume excluded_volume39431 ų
Envelope volume envelope_volume50043 ų
Hydration-shell volume shell_volume18395 ų
Envelope diameter envelope_diameter99.4
Shell Rg shell_rg29.29
Envelope Rg envelope_rg25.13
Shape Rg shape_rg24.19
Total Rg total_rg24.87
Total atoms total_atoms2216
Residues n_residues270
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 dmax92.8
Rg (real space) rg_real25.23
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.6800e+07
I(0) uncertainty (real space) i0_real_error2.8930e+05
Rg (reciprocal space) rg_reciprocal25.17
I(0) (reciprocal space) i0_reciprocal16800000.0000
Solution quality estimate total_estimate0.7011
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3343000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.579; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.376; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4yymA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like
Domain ID domain_id4yymB00
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)