8eqk

Human PU.1 ETS-Domain (165-270) Bound to d(AATAACCGGAAGTGGG)

Method: X-RAY DIFFRACTION Dmax: 55.5 Å Quality: EXCELLENT

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

Transcription factor PU.1

Homo sapiens

UniProt P17947

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 Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain F; UniProt 165–270 Fragment:ETS-Domain UNP residues 165-270 ;DNA (5'-D(*AP*AP*TP*AP*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(*TP*CP*CP*CP*AP*CP*TP*TP*CP*CP*GP*GP*TP*TP*AP*T)-3') ; × 1 NA SODIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;100 mM Sodium Acetate, pH=4.6, 2% PEG 3350 Resolution 1.45 Å R-free 0.179

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.

34 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPI1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–106; UniProt 165–270

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 8eqk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8eqk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8eqk
Deposition date deposition_date2022-10-07
Structure title titleHuman PU.1 ETS-Domain (165-270) Bound to d(AATAACCGGAAGTGGG)
Keywords keywordstranscription factor, protein-DNA complex, ETS family, ETS, PU.1, 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_guinier17.61
Radius of gyration Rg (electron density) rg_electron16.43
Forward intensity I(0) i012118300.00
Molecular weight molecular_weight20283.0 kDa
Excluded volume excluded_volume22893 ų
Envelope volume envelope_volume28730 ų
Hydration-shell volume shell_volume15005 ų
Envelope diameter envelope_diameter56.6
Shell Rg shell_rg22.05
Envelope Rg envelope_rg16.70
Shape Rg shape_rg16.34
Total Rg total_rg17.38
Total atoms total_atoms2513
Residues n_residues123
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 dmax55.5
Rg (real space) rg_real17.53
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.2120e+07
I(0) uncertainty (real space) i0_real_error1.4780e+05
Rg (reciprocal space) rg_reciprocal17.54
I(0) (reciprocal space) i0_reciprocal12120000.0000
Solution quality estimate total_estimate0.9053
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1091000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)