1bc8

STRUCTURES OF SAP-1 BOUND TO DNA SEQUENCES FROM THE E74 AND C-FOS PROMOTERS PROVIDE INSIGHTS INTO HOW ETS PROTEINS DISCRIMINATE BETWEEN RELATED DNA TARGETS

Method: X-RAY DIFFRACTION Dmax: 50.6 Å Quality: EXCELLENT

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

PROTEIN (SAP-1 ETS DOMAIN)

Homo sapiens

UniProt P28324

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 C; UniProt 1–93 Fragment:ETS DOMAIN, RESIDUES 1-93 ;DNA (5'-D(*TP*AP*CP*CP*GP*GP*AP*AP*GP*T)-3') ; × 1 ;DNA (5'-D(*AP*AP*CP*TP*TP*CP*CP*GP*GP*T)-3') ; × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;50 MM NA CACODYLATE (PH 6.0), 5.0% PEG8000, 20 MM ZINC ACETATE Resolution 1.93 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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELK4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–93; UniProt 1–93

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 1bc8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bc8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bc8
Deposition date deposition_date1998-05-05
Structure title titleSTRUCTURES OF SAP-1 BOUND TO DNA SEQUENCES FROM THE E74 AND C-FOS PROMOTERS PROVIDE INSIGHTS INTO HOW ETS PROTEINS DISCRIMINATE BETWEEN RELATED DNA TARGETS
Keywords keywordsETS DOMAIN, DNA-BINDING DOMAIN, WINGED HELIX-TURN-HELIX, DNA-BINDING SPECIFICITY, 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_guinier16.18
Radius of gyration Rg (electron density) rg_electron14.82
Forward intensity I(0) i08046570.00
Molecular weight molecular_weight17414.0 kDa
Excluded volume excluded_volume20321 ų
Envelope volume envelope_volume23467 ų
Hydration-shell volume shell_volume13461 ų
Envelope diameter envelope_diameter49.4
Shell Rg shell_rg20.67
Envelope Rg envelope_rg15.10
Shape Rg shape_rg14.69
Total Rg total_rg16.07
Total atoms total_atoms1196
Residues n_residues113
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 dmax50.6
Rg (real space) rg_real16.09
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real8.0470e+06
I(0) uncertainty (real space) i0_real_error9.1140e+04
Rg (reciprocal space) rg_reciprocal16.10
I(0) (reciprocal space) i0_reciprocal8047000.0000
Solution quality estimate total_estimate0.9042
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.4
Skewness Skewness skewness0.165
Kurtosis Kurtosis kurtosis-0.421
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha849100.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bc8c_
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 (1 domains)

Domain ID domain_id1bc8C00
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)