4zph

Crystal Structure of the Heterodimeric HIF-2a:ARNT Complex with Proflavine

Method: X-RAY DIFFRACTION Dmax: 131.7 Å Quality: GOOD

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

Aryl hydrocarbon receptor nuclear translocator

Mus musculus

UniProt P53762

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 82–464 Fragment:UNP residues 82-464 Endothelial PAS domain-containing protein 1 × 1 (P97481) PRL PROFLAVIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate, pH 7.0, 6% PEG3350 Resolution 2.80 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 82–464 Fragment:UNP residues 82-464 Endothelial PAS domain-containing protein 1 × 1 (P97481) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate, pH 7.0, 6% PEG3350 Resolution 2.80 Å R-free 0.221

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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARNT_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–384; UniProt 82–464 Author chain C; PDBConstruct 2–384; UniProt 82–464

Endothelial PAS domain-containing protein 1

Mus musculus

UniProt P97481

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 3–361 Fragment:UNP residues 3-361 Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) PRL PROFLAVIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate, pH 7.0, 6% PEG3350 Resolution 2.80 Å R-free 0.221
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 3–361 Fragment:UNP residues 3-361 Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;289 K;2% Tacsimate, pH 7.0, 6% PEG3350 Resolution 2.80 Å R-free 0.221

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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EPAS1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–360; UniProt 3–361 Author chain D; PDBConstruct 2–360; UniProt 3–361

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 4zph

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zph
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4zph
Deposition date deposition_date2015-05-07
Structure title titleCrystal Structure of the Heterodimeric HIF-2a:ARNT Complex with Proflavine
Keywords keywordsHIF-2a, ARNT, bHLH-PAS, Proflavine, PROTEIN TRANSPORT-TRANSCRIPTION complex; PROTEIN TRANSPORT/TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.51
Radius of gyration Rg (electron density) rg_electron39.27
Forward intensity I(0) i0245726000.00
Molecular weight molecular_weight126240.0 kDa
Excluded volume excluded_volume157630 ų
Envelope volume envelope_volume217250 ų
Hydration-shell volume shell_volume46913 ų
Envelope diameter envelope_diameter140.6
Shell Rg shell_rg44.11
Envelope Rg envelope_rg38.50
Shape Rg shape_rg39.28
Total Rg total_rg39.54
Total atoms total_atoms8843
Residues n_residues1092
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 dmax131.7
Rg (real space) rg_real39.59
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real2.4570e+08
I(0) uncertainty (real space) i0_real_error4.9900e+06
Rg (reciprocal space) rg_reciprocal39.55
I(0) (reciprocal space) i0_reciprocal245700000.0000
Solution quality estimate total_estimate0.8859
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.8
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24520000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.816

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)