7k1p

Crystal structure of the second bromodomain (BD2) of human TAF1 bound to bromosporine

Method: X-RAY DIFFRACTION Dmax: 60.2 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1501–1635 Not recorded BMF Bromosporine × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M HEPES (pH 7.5), 10% PEG 8,000, 8% Ethylene glycol Resolution 2.45 Å R-free 0.220

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 3–137; UniProt 1501–1635

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 7k1p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k1p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k1p
Deposition date deposition_date2020-09-08
Structure title titleCrystal structure of the second bromodomain (BD2) of human TAF1 bound to bromosporine
Keywords keywordsTAF1, non-BET, BET, kinase inhibitor, ATR, dual BRD-kinase, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.31
Radius of gyration Rg (electron density) rg_electron16.46
Forward intensity I(0) i04714490.00
Molecular weight molecular_weight15550.0 kDa
Excluded volume excluded_volume19409 ų
Envelope volume envelope_volume22550 ų
Hydration-shell volume shell_volume12385 ų
Envelope diameter envelope_diameter58.5
Shell Rg shell_rg21.52
Envelope Rg envelope_rg17.07
Shape Rg shape_rg16.45
Total Rg total_rg17.44
Total atoms total_atoms1093
Residues n_residues130
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 dmax60.2
Rg (real space) rg_real17.41
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real4.7140e+06
I(0) uncertainty (real space) i0_real_error6.0300e+04
Rg (reciprocal space) rg_reciprocal17.40
I(0) (reciprocal space) i0_reciprocal4714000.0000
Solution quality estimate total_estimate0.8374
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.2
Skewness Skewness skewness0.527
Kurtosis Kurtosis kurtosis-0.125
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha936000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.877; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)