9of2

Dimer of HIF-2a-ARNT Heterodimers Complexed on 51-bp HRE/HAS

Method: ELECTRON MICROSCOPY Dmax: 115.5 Å Quality: EXCELLENT

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

Endothelial PAS domain-containing protein 1

Homo sapiens

UniProt Q99814

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 5–361 Chain E; UniProt 5–361 Not recorded 51-nt Hypoxia Response Element (Forward) × 1 51-nt Hypoxia Response Element (Reverse) × 1 Aryl hydrocarbon receptor nuclear translocator × 2 (P27540) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;50mM HEPES, 150mM NaCl, 5mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å

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.

41 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPAS1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 16–372; UniProt 5–361 Author chain E; PDBConstruct 16–372; UniProt 5–361

Aryl hydrocarbon receptor nuclear translocator

Homo sapiens

UniProt P27540

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 × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 91–470 Chain F; UniProt 91–470 Not recorded 51-nt Hypoxia Response Element (Forward) × 1 51-nt Hypoxia Response Element (Reverse) × 1 Endothelial PAS domain-containing protein 1 × 2 (Q99814) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;50mM HEPES, 150mM NaCl, 5mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å

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.

42 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARNT_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–381; UniProt 91–470 Author chain F; PDBConstruct 2–381; UniProt 91–470

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 9of2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9of2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9of2
Deposition date deposition_date2025-04-29
Structure title titleDimer of HIF-2a-ARNT Heterodimers Complexed on 51-bp HRE/HAS
Keywords keywordsComplex, Hypoxia, Transcription, Cancer, Dimer, Higher-ordered, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.81
Radius of gyration Rg (electron density) rg_electron36.63
Forward intensity I(0) i0384448000.00
Molecular weight molecular_weight145790.0 kDa
Excluded volume excluded_volume176940 ų
Envelope volume envelope_volume253970 ų
Hydration-shell volume shell_volume57006 ų
Envelope diameter envelope_diameter117.3
Shell Rg shell_rg43.69
Envelope Rg envelope_rg35.76
Shape Rg shape_rg36.62
Total Rg total_rg37.10
Total atoms total_atoms18914
Residues n_residues1169
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 dmax115.5
Rg (real space) rg_real37.54
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real3.8440e+08
I(0) uncertainty (real space) i0_real_error5.7320e+06
Rg (reciprocal space) rg_reciprocal37.71
I(0) (reciprocal space) i0_reciprocal384500000.0000
Solution quality estimate total_estimate0.9041
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.025
Kurtosis Kurtosis kurtosis-0.593
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32930000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)