3uv4

Crystal Structure of the second bromodomain of human Transcription initiation factor TFIID subunit 1 (TAF1)

Method: X-RAY DIFFRACTION Dmax: 69.5 Å Quality: GOOD

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

second bromodomain of human Transcription initiation factor TFIID subunit 1 (TAF1)

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 Fragment:unp residues 1501-1635 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.056M NaH2PO4 1.344M K2HPO4, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.89 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1501–1635 Fragment:unp residues 1501-1635 EDO 1,2-ETHANEDIOL × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;0.056M NaH2PO4 1.344M K2HPO4, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.89 Å

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 64 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 24–158; UniProt 1501–1635 Author chain B; PDBConstruct 24–158; 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 3uv4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3uv4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3uv4
Deposition date deposition_date2011-11-29
Structure title titleCrystal Structure of the second bromodomain of human Transcription initiation factor TFIID subunit 1 (TAF1)
Keywords keywordsStructural Genomics Consortium, SGC, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.60
Radius of gyration Rg (electron density) rg_electron19.62
Forward intensity I(0) i014830900.00
Molecular weight molecular_weight28865.0 kDa
Excluded volume excluded_volume36025 ų
Envelope volume envelope_volume42713 ų
Hydration-shell volume shell_volume18671 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg25.50
Envelope Rg envelope_rg19.99
Shape Rg shape_rg19.63
Total Rg total_rg20.43
Total atoms total_atoms2031
Residues n_residues251
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 dmax69.5
Rg (real space) rg_real20.54
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.4830e+07
I(0) uncertainty (real space) i0_real_error1.9830e+05
Rg (reciprocal space) rg_reciprocal20.55
I(0) (reciprocal space) i0_reciprocal14830000.0000
Solution quality estimate total_estimate0.8034
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3506000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3uv4a1
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.2 — Bromodomain
Family Family familya.29.2.0 — automated matches
Domain ID domain_idd3uv4a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3uv4b1
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.2 — Bromodomain
Family Family familya.29.2.0 — automated matches
Domain ID domain_idd3uv4b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3uv4A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like
Domain ID domain_id3uv4B00
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)