3wu0

Crystal structure of phosphorylated ETS-1 DNA binding and autoinhibitory domains (276-441)

Method: X-RAY DIFFRACTION Dmax: 80.7 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 276–441 Chain B; UniProt 276–441 Fragment:UNP RESIDUES 276-441 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;5% PEG 3000, 25% MPD, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP Resolution 2.60 Å R-free 0.277

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–166; UniProt 276–441 Author chain B; PDBConstruct 1–166; UniProt 276–441

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 3wu0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3wu0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3wu0
Deposition date deposition_date2014-04-21
Structure title titleCrystal structure of phosphorylated ETS-1 DNA binding and autoinhibitory domains (276-441)
Keywords keywords;PHOSPHORYLATION, TRANSCRIPTION, ETS-1, AUTOINHIBITION, ETS DOMAIN, DNA-BINDING, ISOPEPTIDE BOND, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE, TRANSCRIPTION REGULATION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.08
Radius of gyration Rg (electron density) rg_electron23.17
Forward intensity I(0) i016767400.00
Molecular weight molecular_weight32021.0 kDa
Excluded volume excluded_volume40450 ų
Envelope volume envelope_volume51482 ų
Hydration-shell volume shell_volume19380 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg29.09
Envelope Rg envelope_rg22.66
Shape Rg shape_rg23.17
Total Rg total_rg23.95
Total atoms total_atoms2263
Residues n_residues276
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 dmax80.7
Rg (real space) rg_real24.14
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.6770e+07
I(0) uncertainty (real space) i0_real_error2.3080e+05
Rg (reciprocal space) rg_reciprocal24.13
I(0) (reciprocal space) i0_reciprocal16770000.0000
Solution quality estimate total_estimate0.7920
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2800000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.919; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3wu0a_
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_idd3wu0b_
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_id3wu0A00
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_id3wu0B00
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)