5nj8

Structural basis for aryl hydrocarbon receptor mediated gene activation

Method: X-RAY DIFFRACTION Dmax: 92.0 Å Quality: EXCELLENT

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

Aryl hydrocarbon receptor

Homo sapiens

UniProt P35869

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 × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 23–273 Not recorded Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) ;DNA (5'-D(*GP*GP*TP*CP*AP*CP*GP*CP*AP*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*GP*TP*TP*GP*CP*GP*TP*GP*AP*CP*C)-3') ; × 1 ER3 ERBIUM (III) ION × 7 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.6;277 K;10 mM HEPES/NaOH pH 6.8, 18% PEG3350, 200 mM ammonium formate Resolution 3.30 Å R-free 0.333
2 Protein–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 23–273 Not recorded Aryl hydrocarbon receptor nuclear translocator × 1 (P53762) ;DNA (5'-D(*GP*GP*TP*CP*AP*CP*GP*CP*AP*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*GP*TP*TP*GP*CP*GP*TP*GP*AP*CP*C)-3') ; × 1 ER3 ERBIUM (III) ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.6;277 K;10 mM HEPES/NaOH pH 6.8, 18% PEG3350, 200 mM ammonium formate Resolution 3.30 Å R-free 0.333

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AHR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–254; UniProt 23–273 Author chain C; PDBConstruct 4–254; UniProt 23–273

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–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain B; UniProt 85–345 Mutation:C256S Aryl hydrocarbon receptor × 1 (P35869) ;DNA (5'-D(*GP*GP*TP*CP*AP*CP*GP*CP*AP*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*GP*TP*TP*GP*CP*GP*TP*GP*AP*CP*C)-3') ; × 1 ER3 ERBIUM (III) ION × 7 ACT ACETATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.6;277 K;10 mM HEPES/NaOH pH 6.8, 18% PEG3350, 200 mM ammonium formate Resolution 3.30 Å R-free 0.333
2 Protein–DNA Heteromer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain D; UniProt 85–345 Mutation:C256S Aryl hydrocarbon receptor × 1 (P35869) ;DNA (5'-D(*GP*GP*TP*CP*AP*CP*GP*CP*AP*AP*CP*C)-3') ; × 1 ;DNA (5'-D(*GP*GP*TP*TP*GP*CP*GP*TP*GP*AP*CP*C)-3') ; × 1 ER3 ERBIUM (III) ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.6;277 K;10 mM HEPES/NaOH pH 6.8, 18% PEG3350, 200 mM ammonium formate Resolution 3.30 Å R-free 0.333

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 B; PDBConstruct 7–239; UniProt 85–345 Author chain D; PDBConstruct 7–239; UniProt 85–345

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 5nj8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5nj8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5nj8
Deposition date deposition_date2017-03-28
Structure title titleStructural basis for aryl hydrocarbon receptor mediated gene activation
Keywords keywordsbasic helix loop helix PAS domain transcription factor, transcription; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.66
Radius of gyration Rg (electron density) rg_electron29.25
Forward intensity I(0) i0159944000.00
Molecular weight molecular_weight85653.0 kDa
Excluded volume excluded_volume100490 ų
Envelope volume envelope_volume141520 ų
Hydration-shell volume shell_volume39893 ų
Envelope diameter envelope_diameter91.7
Shell Rg shell_rg36.74
Envelope Rg envelope_rg28.99
Shape Rg shape_rg29.18
Total Rg total_rg30.05
Total atoms total_atoms10871
Residues n_residues708
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 dmax92.0
Rg (real space) rg_real30.46
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.5990e+08
I(0) uncertainty (real space) i0_real_error2.2020e+06
Rg (reciprocal space) rg_reciprocal30.55
I(0) (reciprocal space) i0_reciprocal160000000.0000
Solution quality estimate total_estimate0.9121
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.048
Kurtosis Kurtosis kurtosis-0.611
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24570000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5nj8A01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily10 — Helix-loop-helix DNA-binding domain
Domain ID domain_id5nj8B01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily10 — Helix-loop-helix DNA-binding domain
Domain ID domain_id5nj8B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id5nj8D01
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology280 — MYOD Basic-Helix-Loop-Helix Domain, subunit B
Homologous superfamily homologous superfamily10 — Helix-loop-helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)