3ri4

Ets1 cooperative binding to widely separated sites on promoter DNA

Method: X-RAY DIFFRACTION Dmax: 78.4 Å Quality: EXCELLENT

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

Isoform Ets-1 p27 of Protein C-ets-1

Homo sapiens

UniProt P14921

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–DNA Homooligomer Protein × 2 DNA 4 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 64–225 Chain D; UniProt 64–225 Fragment:UNP residues 280-441 TCR alpha promoter DNA × 2 TCR alpha promoter DNA × 2 X-RAY DIFFRACTION X-ray crystallization conditions:sitting drop vapor diffusion and macroseeding;pH 8.5;295 K;200 mM ammonium chloride, 10 mM calcium chloride, 50 mM Tris-HCl buffer (pH 8.5), 18.5% v/v PEG MME 2000, 3% v/v glycerol, sitting drop vapor diffusion and macroseeding, temperature 295K Resolution 3.00 Å R-free 0.284

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.

20 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ETS1_HUMAN
Isoform P14921-4
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–163; UniProt 64–225 Author chain D; PDBConstruct 2–163; UniProt 64–225

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 3ri4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ri4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ri4
Deposition date deposition_date2011-04-12
Structure title titleEts1 cooperative binding to widely separated sites on promoter DNA
Keywords keywords;transcription, T-cell receptor alpha, DNA binding, autoinhibition, Ets domain, transcription factor, DNA, Runx2, Runx1, Transcription-DNA complex ;; Transcription/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.90
Radius of gyration Rg (electron density) rg_electron23.82
Forward intensity I(0) i065178000.00
Molecular weight molecular_weight51188.0 kDa
Excluded volume excluded_volume58893 ų
Envelope volume envelope_volume75628 ų
Hydration-shell volume shell_volume26786 ų
Envelope diameter envelope_diameter82.0
Shell Rg shell_rg30.56
Envelope Rg envelope_rg23.44
Shape Rg shape_rg23.77
Total Rg total_rg24.58
Total atoms total_atoms3534
Residues n_residues336
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 dmax78.4
Rg (real space) rg_real24.78
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real6.5180e+07
I(0) uncertainty (real space) i0_real_error9.1750e+05
Rg (reciprocal space) rg_reciprocal24.81
I(0) (reciprocal space) i0_reciprocal65180000.0000
Solution quality estimate total_estimate0.9032
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.195
Kurtosis Kurtosis kurtosis-0.385
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5044000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.915; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3ri4a_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.21 — ets domain
Domain ID domain_idd3ri4d_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.5 — 'Winged helix' DNA-binding domain
Family Family familya.4.5.21 — ets domain

CATH v4.4 (2 domains)

Domain ID domain_id3ri4A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain
Domain ID domain_id3ri4D00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)