9ynz

Human PU.1 ETS-Domain (165-270) Bound to d(5'-AATAAGCGGAAGTGGG-3') d(5'-TCCCACT*CPD*CGCTTAT-3')

Method: X-RAY DIFFRACTION Dmax: 55.3 Å Quality: GOOD

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*GP*CP*GP*GP*AP*AP*GP*TP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*AP*CP*T*(CPD)P*CP*GP*CP*TP*TP*AP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;293 K;2% PEG 3350, 100 mM Sodium Acetate, pH 4.6 Resolution 2.05 Å R-free 0.244

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 9ynz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ynz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ynz
Deposition date deposition_date2025-10-13
最后修订 last_revision2025-10-22
Structure title titleHuman PU.1 ETS-Domain (165-270) Bound to d(5'-AATAAGCGGAAGTGGG-3') d(5'-TCCCACT*CPD*CGCTTAT-3')
Keywords keywordstranscription factor, protein-DNA complex, ETS family, ETS, PU.1, TRANSCRIPTION-DNA complex, DNA mismatch, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.29
Radius of gyration Rg (electron density) rg_electron16.10
Forward intensity I(0) i011909700.00
Molecular weight molecular_weight20062.0 kDa
Excluded volume excluded_volume22635 ų
Envelope volume envelope_volume28167 ų
Hydration-shell volume shell_volume14886 ų
Envelope diameter envelope_diameter56.8
Shell Rg shell_rg21.86
Envelope Rg envelope_rg16.40
Shape Rg shape_rg16.02
Total Rg total_rg17.08
Total atoms total_atoms2495
Residues n_residues120
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 dmax55.3
Rg (real space) rg_real17.21
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.1910e+07
I(0) uncertainty (real space) i0_real_error1.3940e+05
Rg (reciprocal space) rg_reciprocal17.22
I(0) (reciprocal space) i0_reciprocal11910000.0000
Solution quality estimate total_estimate0.8236
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1319000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)