9mx8

Crystal structure of the DNA binding domain of FLI1 in complex with a DNA containing three contiguous GGAA sites

Method: X-RAY DIFFRACTION Dmax: 74.5 Å Quality: GOOD

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

Friend leukemia integration 1 transcription factor

Homo sapiens

UniProt Q01543

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 × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 259–375 Chain C; UniProt 259–375 Chain D; UniProt 259–375 Fragment:DNA-binding domain (residues 259-375) Mutation:F362A ;DNA (5'-D(P*GP*AP*CP*CP*GP*GP*AP*AP*GP*GP*AP*AP*GP*GP*AP*AP*GP*TP*G)-3') ; × 1 ;DNA (5'-D(*CP*AP*CP*TP*TP*CP*CP*TP*TP*CP*CP*TP*TP*CP*CP*GP*GP*TP*C)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M sodium cacodylate, pH 7.0, 1.6 M sodium acetate, added cryoprotectant: 34% sucrose Resolution 3.15 Å R-free 0.278

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.

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FLI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–121; UniProt 259–375 Author chain C; PDBConstruct 5–121; UniProt 259–375 Author chain D; PDBConstruct 5–121; UniProt 259–375

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 9mx8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mx8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mx8
Deposition date deposition_date2025-01-17
Structure title titleCrystal structure of the DNA binding domain of FLI1 in complex with a DNA containing three contiguous GGAA sites
Keywords keywordsoncogene, Ewing sarcoma, transcription factor, microsatellite, DNA BINDING PROTEIN-DNA complex, DNA BINDING PROTEIN; DNA BINDING PROTEIN/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.10
Radius of gyration Rg (electron density) rg_electron22.61
Forward intensity I(0) i048525600.00
Molecular weight molecular_weight45903.0 kDa
Excluded volume excluded_volume53897 ų
Envelope volume envelope_volume68312 ų
Hydration-shell volume shell_volume25126 ų
Envelope diameter envelope_diameter75.1
Shell Rg shell_rg29.47
Envelope Rg envelope_rg22.90
Shape Rg shape_rg22.63
Total Rg total_rg23.27
Total atoms total_atoms3190
Residues n_residues338
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 dmax74.5
Rg (real space) rg_real23.05
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real4.8530e+07
I(0) uncertainty (real space) i0_real_error6.4160e+05
Rg (reciprocal space) rg_reciprocal23.06
I(0) (reciprocal space) i0_reciprocal48530000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha8938000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)