6vge

Crystal structure of the DNA binding domains of human transcription factor ERG, human Runx2 bound to core binding factor beta (Cbfb), in complex with 16mer DNA CAGAGGATGTGGCTTC

Method: X-RAY DIFFRACTION Dmax: 87.5 Å Quality: GOOD

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

Transcriptional regulator ERG

Homo sapiens

UniProt P11308

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 313–426 Fragment:DNA binding domain ;DNA (5'-D(P*CP*AP*GP*AP*GP*GP*AP*TP*GP*TP*GP*GP*CP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*GP*CP*CP*AP*CP*AP*TP*CP*CP*TP*CP*TP*G)-3') ; × 1 Runt-related transcription factor 2 × 1 (Q13950) Core-binding factor subunit beta × 1 (Q13951) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.6 M K/Na Tartrate, 0.1 M Hepes, pH7.0 Resolution 4.25 Å R-free 0.317

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ERG_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–118; UniProt 313–426

Runt-related transcription factor 2

Homo sapiens

UniProt Q13950

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain D; UniProt 111–287 Fragment:DNA binding domain Transcriptional regulator ERG × 1 (P11308) ;DNA (5'-D(P*CP*AP*GP*AP*GP*GP*AP*TP*GP*TP*GP*GP*CP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*GP*CP*CP*AP*CP*AP*TP*CP*CP*TP*CP*TP*G)-3') ; × 1 Core-binding factor subunit beta × 1 (Q13951) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.6 M K/Na Tartrate, 0.1 M Hepes, pH7.0 Resolution 4.25 Å R-free 0.317

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUNX2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–177; UniProt 111–287

Core-binding factor subunit beta

Homo sapiens

UniProt Q13951

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 Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain G; UniProt 1–142 Fragment:DNA binding domain Transcriptional regulator ERG × 1 (P11308) ;DNA (5'-D(P*CP*AP*GP*AP*GP*GP*AP*TP*GP*TP*GP*GP*CP*TP*TP*C)-3') ; × 1 ;DNA (5'-D(P*GP*AP*AP*GP*CP*CP*AP*CP*AP*TP*CP*CP*TP*CP*TP*G)-3') ; × 1 Runt-related transcription factor 2 × 1 (Q13950) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.6 M K/Na Tartrate, 0.1 M Hepes, pH7.0 Resolution 4.25 Å R-free 0.317

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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PEBB_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 15–156; UniProt 1–142

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 6vge

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6vge
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6vge
Deposition date deposition_date2020-01-07
Structure title titleCrystal structure of the DNA binding domains of human transcription factor ERG, human Runx2 bound to core binding factor beta (Cbfb), in complex with 16mer DNA CAGAGGATGTGGCTTC
Keywords keywordsEwing sarcoma, enhancer, transcription factor, oncogenesis, prostate cancer, ETS-family, Runt-family, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.34
Radius of gyration Rg (electron density) rg_electron25.98
Forward intensity I(0) i051824200.00
Molecular weight molecular_weight48350.0 kDa
Excluded volume excluded_volume57248 ų
Envelope volume envelope_volume77100 ų
Hydration-shell volume shell_volume25670 ų
Envelope diameter envelope_diameter91.2
Shell Rg shell_rg32.23
Envelope Rg envelope_rg25.68
Shape Rg shape_rg25.98
Total Rg total_rg26.61
Total atoms total_atoms3361
Residues n_residues368
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 dmax87.5
Rg (real space) rg_real26.41
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real5.1820e+07
I(0) uncertainty (real space) i0_real_error8.6810e+05
Rg (reciprocal space) rg_reciprocal26.39
I(0) (reciprocal space) i0_reciprocal51820000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.343
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4718000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.882; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)