7vni

AHR-ARNT PAS-B heterodimer

Method: X-RAY DIFFRACTION Dmax: 85.3 Å Quality: REASONABLE

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

Ahr homolog spineless

Drosophila melanogaster

UniProt O61543

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 264–381 Not recorded Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium arsenate (pH 6.5), 0.2 M MgCl2, 2 M (NH4)2SO4 Resolution 2.00 Å R-free 0.219
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 264–381 Not recorded Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium arsenate (pH 6.5), 0.2 M MgCl2, 2 M (NH4)2SO4 Resolution 2.00 Å R-free 0.219

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.

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

View Construct and Data Evidence
UniProt name O61543_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–120; UniProt 264–381 Author chain B; PDBConstruct 3–120; UniProt 264–381

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 D; UniProt 358–466 Not recorded Ahr homolog spineless × 1 (O61543) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium arsenate (pH 6.5), 0.2 M MgCl2, 2 M (NH4)2SO4 Resolution 2.00 Å R-free 0.219
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 358–466 Not recorded Ahr homolog spineless × 1 (O61543) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium arsenate (pH 6.5), 0.2 M MgCl2, 2 M (NH4)2SO4 Resolution 2.00 Å R-free 0.219

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 2
Chains and sequence ranges Author chain C; PDBConstruct 3–111; UniProt 358–466 Author chain D; PDBConstruct 3–111; UniProt 358–466

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 7vni

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7vni
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7vni
Deposition date deposition_date2021-10-11
Structure title titleAHR-ARNT PAS-B heterodimer
Keywords keywordstranscription factor, ligand binding domain, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.98
Radius of gyration Rg (electron density) rg_electron26.32
Forward intensity I(0) i043559600.00
Molecular weight molecular_weight50685.0 kDa
Excluded volume excluded_volume63080 ų
Envelope volume envelope_volume79088 ų
Hydration-shell volume shell_volume25656 ų
Envelope diameter envelope_diameter82.5
Shell Rg shell_rg32.84
Envelope Rg envelope_rg26.09
Shape Rg shape_rg26.31
Total Rg total_rg27.03
Total atoms total_atoms3565
Residues n_residues432
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 dmax85.3
Rg (real space) rg_real26.98
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real4.3560e+07
I(0) uncertainty (real space) i0_real_error6.3900e+05
Rg (reciprocal space) rg_reciprocal26.99
I(0) (reciprocal space) i0_reciprocal43560000.0000
Solution quality estimate total_estimate0.6429
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.678
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14600000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 0.199; Positv: 1.000; Valcen: 0.934; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)